The characteristic of most lipases is the interfacial activation at a lipid interface or in non-polar solvents. Interfacial activation is linked to a large conformational change of a lid, from a closed to an open conformation which makes the active site accessible for substrates. While for many lipases crystal structures of the closed and open conformation have been determined, the pathway of the conformational transition and possible bottlenecks are unknown. Therefore, molecular dynamics simulations of a closed homology model and an open crystal structure of Burkholderia cepacia lipase in water and toluene were performed to investigate the influence of solvents on structure, dynamics, and the conformational transition of the lid.
The conformational transition of B. cepacia lipase was dependent on the solvent. In simulations of closed B. cepacia lipase in water no conformational transition was observed, while in three independent simulations of the closed lipase in toluene the lid gradually opened during the first 10–15 ns. The pathway of conformational transition was accessible and a barrier was identified, where a helix prevented the lid from opening to the completely open conformation. The open structure in toluene was stabilized by the formation of hydrogen bonds.
In simulations of open lipase in water, the lid closed slowly during 30 ns nearly reaching its position in the closed crystal structure, while a further lid opening compared to the crystal structure was observed in toluene. While the helical structure of the lid was intact during opening in toluene, it partially unfolded upon closing in water. The closing of the lid in water was also observed, when with eight intermediate structures between the closed and the open conformation as derived from the simulations in toluene were taken as starting structures. A hydrophobic β-hairpin was moving away from the lid in all simulations in water, which was not observed in simulations in toluene. The conformational transition of the lid was not correlated to the motions of the β-hairpin structure.
Conformational transitions between the experimentally observed closed and open conformation of the lid were observed by multiple molecular dynamics simulations of B. cepacia lipase. Transitions in both directions occurred without applying restraints or external forces. The opening and closing were driven by the solvent and independent of a bound substrate molecule.
Burkholderia cepacia lipase (BCL) formerly known as Pseudomonas cepacia lipase has been shown to be a useful enzyme which catalyzes a broad range of different reactions in water and non-polar solvents under mild conditions. BCL is a highly selective catalyst for a broad range of substrates , including the kinetic resolution of racemic mixtures of secondary alcohols by hydrolysis in water or esterification in organic solvents [2–4]. All lipases have a similar architecture, the α/β hydrolase fold [5, 6], which consists of parallel β-strands flanked by α-helices, and an active site with a catalytic triad consisting of Ser, His, and Asp/Glu [6, 7]. The characteristic of most lipases is their activation upon binding to a hydrophobic interface . Most lipases consist of a mobile element at the surface, a lid, which covers the active site . The lid is opening at a hydrophobic interface, making the active site accessible for substrates and enhancing the activity of the lipase [10, 11]. Because the exterior of the lid is hydrophilic and its interior is hydrophobic, the hydrophobic surface of lipases increases upon lid opening . Therefore, in non-polar solvents the open conformation was expected to be thermodynamically favored .
The crystal structure of BCL has been determined without a bound inhibitor in an open conformation of the lid. The lid consists of a helix-loop-helix motif with helix α4 (residues 118–127) and helix α5 (residues 134–150) which are linked to helix α6 (residues 160–166) . BCL contains an essential Ca2+-ion site  which stabilizes a β-hairpin (residues 214–228) . While no experimental structure of BCL in the closed conformation is available, a homologous lipase from Burkholderia glumae (BGL) [PDB: 1QGE]  with a sequence identity of 84% has been crystallized in the closed conformation. The cores of both homologous lipases have an identical structure with a root-mean squared deviation (RMSD) of backbone atoms of 0.7 Å, while the main structural difference between the two conformations is the position of the lid (residues 118–150) with a RMSD of 5 Å. The length of helix α5 in BCL (residues 134–150) was identified to be longer compared to BGL (residues 136–150), and the length of helix α6 in BCL (residues 160–166) was shorter in BGL (residues 156–166). Thus, the X-ray structures of open BCL and closed BGL suggests that the interfacial activation of BCL involves a motion of helices α4 and α5  and a partial unfolding of helix α6 in BGL. However, the mechanism of lid opening is still discussed. Several mechanisms of interfacial activation of lipases have been supposed. The substrate theory suggests that the lid opening is induced by binding of a substrate [18, 19], while the enzyme theory suggests that the lid opens by adsorption to a hydrophobic interface . Despite the fact that structures of the closed [9, 13, 17, 20] and the open conformation [20–25] of several lipases are known, a complete description of the mechanism of lid opening and closing is still lacking. The identification of mobile elements was possible by the availability of open and closed structures, but attempts to obtain any intermediates between the closed and open conformation  and conformational transitions have not been successful in experiment. Therefore, short molecular dynamics simulations of different lipases have been reported to get more insight into the conformational transition of the lid [26–31]. However, the time-scale of conformational transition of the lid from the closed to the fully open conformation was not reached in short molecular dynamics simulations. Therefore, methods like essential dynamics , normal mode analysis , and Brownian dynamics simulations  were used to study the lid opening in non-polar solvents.
To investigate the solvent-dependent motions of the mobile lid (residues 118–150) and the β-hairpin (residues 214–228) of BCL, multiple molecular dynamics simulations of the open crystal structure and the closed homology model of BCL were performed in water and toluene without using restraints or external forces. Toluene was used as a typical non-polar solvent which is widely used in lipase-catalyzed conversions. It has been shown that BCL is stable in toluene without significant loss of activity. The details of the conformational pathway were examined, to distinguish whether the transition occurs via a rigid-body movement or via a partial or complete unfolding, and bottlenecks in the lid opening and closing were identified.
Three simulations of 15–30 ns with different starting velocity distributions were performed for four enzyme-solvent systems, the closed homology model and the open crystal structure of BCL in water and toluene. The observed conformational transitions of the lid were dependent on the solvent, while all three simulations of the same enzyme-solvent system showed essentially the same transition. In eleven simulations, the Ca2+-binding site was stable, while in one simulation of closed BCL in water the Ca2+-ion left the binding pocket after 26 ns of simulation time.
All available crystal structures of BCL have been obtained in their open conformation [14, 23, 24, 35, 36] showing only small root mean squared deviations (RMSD) of backbone atoms in the range of 0.2–0.5 Å. In all crystal structures there are crystal contacts between helix α4 (residues 118–127) and helix α9 (residues 243–256) of a second monomer, as well as between residues 217–218 and 223–225 of the β-hairpin and residues 130–138 of helix α5 of the lid of a second monomer (additional file 1). The crystal contacts are stabilized by electrostatic interactions between the negative potential of the lid and the positive potential of the β-hairpin (data not shown). In addition, hydrophobic contacts were observed between helix α5 and its equivalent of a second monomer at residues 142 to 149. In contrast, there are no crystal contacts between the lid and the β-hairpin in the crystal structure in the closed conformation of the homologous Burkholderia glumae lipase (BGL) [PDB: 1QGE] , which was used as template for the homology model of closed BCL. The sequences of BCL and BGL are highly similar with a sequence identity of 84%. In the lid, only residues 125, 128, 129, 148, and 150 are different.
The homology model of closed BCL showed no significant differences to the core of the open crystal structure, but was different in the conformation of the lid. The major movement was expected for helix α5 and the loop between helices α4 and α5, while helix α4 slightly changed its orientation. Helix α5 of BCL increased in length in the open conformation (residues 134–150) as compared to the closed conformation (residues 136–150), while helix α6 decreased in length in the open conformation (residues 160–166) as compared to the closed conformation (residue 156–166) of BCL (figure 1), as already been observed in the closed conformation of BGL. Furthermore, small differences can be observed in the position of the β-hairpin and in other loops (residues 17–27 and residues 50–59). The quality of the closed homology model of BCL was analyzed by ProSA showing a Z-score of -5.9 and a local model quality similar to the template BGL with a Z-score of -6.7. In contrast, the Z-scores of both closed structures were slightly better as compared to the open crystal structure of BCL showing a Z-score of -4.9 and a local model quality with high energy at helix α5 of the lid.
Structure of open and closed BCL. The open and closed conformation of BCL is shown in a cartoon representation. The lid of the open crystal structure of BCL [PDB: 3LIP] is colored blue and of the closed homology model green, the sphere of the Ca2+-ion is colored yellow. The catalytic triad consisting of Ser, His, and Asp is colored red. For analysis distances were measured between atom Cα of residue 132 from the simulated to the initial structure, respectively.
The conformation of the lid was characterized by two distances: the movement of the whole lid was described by the distance between atom Cα of residue 138 in helix α5 to atom Cα of residue 250 in helix α9, which was 6.1 Å in the closed homology model and 24.5 Å in the open crystal structure. The movement of the loop between helices α4 and α5 was described by the distance of atom Cα of residue 132 from the closed to the open conformation, which was 11.1 Å between the homology model and the crystal structure.
In all three simulations of closed BCL in water no significant conformational change was observed. The backbone RMSD of the conformation after 30 ns to the initial structure was 1.3 Å of the core and 2.0 Å of the lid. The core was stable, deviations were mainly observed at surface loops, especially at the β-hairpin (residues 214–228) and the loop between helices α4 and α5 of the lid (residues 129–133). The lid was slightly closing as indicated by the distance Cα 138-Cα 250 which decreased from 6.4 Å to 6.1 Å and the movement of the loop between helices α4 and α5 of the lid by a distance of 5.7 Å between atom Cα of residue 132 from the simulated to the initial structure. The position of helix α5 (residues 134–150) was unchanged, helix α4 (residues 118–127) showed a movement by 2.7 Å at its C-cap, near the loop between helices α4 and α5.
The calculated B-factors per residue identified helix α5, the loop between helix α4 and α5, the β-hairpin, helix α6 (residues 156–159), helix α7 (residues 170–178) and five further surface loops (loop 23–28, loop 48–61, loop 184–193, loop 198–203, loop 232–240) as the most flexible regions (figure 2). While the lid showed only a small movement, the flexible hydrophobic β-hairpin moved away from the lid by up to 9.7 Å (average of three simulations: 7.6 Å), measured by the distance of atom Cα 221 to its initial structure. Thus, the movement of the β-hairpin was independent of the movement of the lid.
Flexibility of closed BCL in water. The flexibility of the closed conformation of BCL in water, indicated by calculated B-factors per residue [Å2], was calculated from the last 10 ns of simulation.
In all three simulations of open BCL in toluene, the core was stable, while the lid opened slightly more (figure 3), as compared to the crystal structure. The backbone RMSD of the conformation after 30 ns to the initial structure was 1.0 Å of the core and 2.4 Å of the lid. The distance Cα 138-Cα 250 increased by 3 Å from 24.3 Å to 27.3 Å, indicating a further lid opening. The distance of atom Cα of residue 132 in the loop between helix α4 and α5 from the initial structure to the simulated structure was 10.7 Å, indicating a major movement of the loop. In contrast to the simulations of the closed structure in water, the flexible β-hairpin did not shift. During the further lid opening, the hydrophobic surface increased by 80 Å2 as compared to the crystal structure. The regions with highest flexibility as indicated by the calculated B-factors per residue were the lid, the β-hairpin, and further surface loops (residues 23–28, 185–189, 198–203, 232–240) (figure 4).
Structure of open BCL in toluene. The open crystal structure of BCL (green) in a cartoon representation showed a further lid opening after simulation of 30 ns in toluene (red).
Flexibility of open BCL in toluene. The flexibility of the open conformation of BCL in toluene, indicated by calculated B-factors per residue [Å2], was calculated from the last 10 ns of the simulation in toluene.
In all three simulations of closed BCL in toluene, the lid gradually opened [additional file 2], while the core of the protein was stable. The backbone RMSD of the conformation after 30 ns to the initial structure was 1.3 Å of the core and 4.8 Å of the lid. The RMSD to the initial structure continuously increased during the first 13 ns of simulation (figure 5) by a fast opening of the lid (figure 6), while the distance Cα 138-Cα 250 increased by 17 Å. Between 13 and 22 ns the lid slightly opened further by a distance Cα 138-Cα 250 of 2 Å, approaching its position in the nearly open conformation of the crystal structure until reaching a barrier (additional file 3). After gradually opening, the movement of the lid was blocked by helix α6 at a distance Cα 138-Cα 250 of 23.2 Å, near to its position in the crystal structure with a distance Cα 138-Cα 250 of 24.5 Å. The movement of helix α5 was blocked by the N-cap of helix α6 (residues 156 to 159) (figure 7) and it was not possible to overcome this barrier until the end of simulations. While in the simulation residues 156 to 159 were helical as in the homology model of the closed structure, helix α6 (residues 160–166) in the crystal structure of the open conformation was partially unfolded near its N-cap, leaving residues 156 to 159 in a loop structure (additional file 4), which would allow the further movement of helix α5.
RMSD in simulations of closed BCL in toluene. Root mean squared deviations (RMSD) of backbone atoms of the core and the flexible lid as a function of time during simulation of 30 ns of closed BCL in toluene starting from the closed homology model.
Movement of the lid of closed BCL in toluene. The movement of the lid of closed BCL as a function of time during the simulation of 30 ns in toluene was measured by the distance Cα 138-Cα 250. The lid was opening about 18 Å from the closed to the open conformation.
Barrier during opening of the lid. The movement of helix α5 (residues 134 to 150) was blocked by helix α6 (residues 156 to 166) during simulation of closed BCL in toluene (B) from their starting conformation (A). The unfolding of residues 156 to 159 of helix α6 would be necessary for the complete movement of the lid (C).
In all simulations in toluene, a salt bridge was formed between Asp121 at the N-cap of helix α4 and Arg258, which was not observed in the crystal structures of BCL and the homology model derived from BGL. This salt bridge prevented helix α4 from a movement in toluene. The opening of the lid was a hinge-type motion of a single helix α5 and the concomitant stretching of the flexible loop between helix α4 and α5. During the conformational transition the secondary structure of helix α5 was conserved. Thus, the lid opening involved conformational rearrangements of several secondary structure elements: a rigid body movement of helix α5 and a movement of the loop between helix α4 and α5, while helix α4 showed no significant movement (figure 8). The solvent accessible surface area (SASA) of the open crystal structure (13309 Å2) was 300 Å2 larger than the SASA of the closed conformation of the homology model (12978 Å2). During lid opening, the SASA increased by 800 Å2 to 13803 Å2. While the hydrophilic SASA decreased by 300 Å2, the hydrophobic SASA increased by 1100 Å2 exposing a large hydrophobic patch of the lid to the non-polar solvent (residues Phe119, Val123, Val126, Val138, Ile139, Phe142, Val143, Val145, Phe146, and Leu149). The increase in hydrophobic SASA mainly occurred during the first 13 ns in correlation with lid opening (figure 9). While in the closed structure this hydrophobic patch was shielded from the solvent, making the protein surface more hydrophilic (additional file 5), in the open conformation the hydrophobic interior of the lid was exposed to the solvent.
Conformations of closed BCL during conformational transition. Conformations of closed BCL (grey) in a cartoon representation during gradually lid opening (blue) in simulation of 30 ns in toluene (A) at the beginning and (B) after 3 ns, (C) 7 ns, (D) 10 ns, (E) 17 ns and, (F) 30 ns.
Hydrophobic surface during conformational transition. The hydrophobic surface of BCL during the 30 ns simulation of closed conformation in toluene is represented as a function of time. The hydrophobic surface increased by 1100 Å2 by lid opening.
The β-hairpin was very flexible, but showed no directed movement in contrast to the simulations in water.
In the three simulations of open BCL in water, a partial lid closing was observed, while the core of the protein was stable. The backbone RMSD of the conformation after 30 ns to the initial structure of open BCL was 0.7 Å of the core and 3.1 Å of the lid. The distance Cα 138-Cα 250 decreased by 5.8 Å, from 24.4 Å to 18.6 Å. The distance of atom Cα of residue 132 in the loop between helix α4 and α5 to its position in the open crystal structure increased to 12.3 Å. However, the fully closed conformation was not reached. Predominantly helix α5 was moving, while helices α4, α6, and α9 showed no movement. The movement of helix α5 was very slow and was not blocked by other structural elements. In contrast to the opening in toluene, helix α5 partially unfolded at its N-cap (residues 134–138) and changed from a straight to a more curved structure. As in the simulations of closed BCL in water, the β-hairpin showed a movement away from the lid by up to 7.2 Å (average of three simulations: 5.3 Å).
To investigate whether the solvent is the only driving force for the observed conformational transition, eight simulations in water were performed starting with intermediate structures taken from the simulation of the lid opening in toluene. Conformers were taken at 6, 9, 12, 15, 18, 21, 24, and 27 ns and simulated for 6 ns after changing the solvent from toluene to water (figure 10A). In all simulations, the lid was partially closing and the distance Cα 138-Cα 250 changed between 1.9 to 14.2 Å (table 1), indicating that the conformational transition can be reversed by changing the solvent. In one simulation, using the conformer after 15 ns as starting structure, the lid closed completely after 6 ns. There was no blocking of the lid by other structural elements in the simulations. It is quite remarkable, that for all simulations in water four preferred distances Cα 138-Cα 250 were identified at 6, 10, 14 and 16.5 Å (figure 10B).
Reverses simulations in toluene. (A) After simulation of open BCL the lid opening of BCL in toluene was reversed in simulations of 6 ns in water, represented as a function of time. The open crystal structure (magenta) and several conformations from the previous lid opening (red, green, blue) in the simulation of closed BCL in toluene (black) were closing again after changing the solvent to water. The lid closing of BCL was measured by the distance between atoms Cα 138 and Cα 250. (B) The frequency of the distance between atoms Cα 138 and Cα 250 in the reversed movement of the lid in water was analyzed. Frequently occurring distances are 6, 10, 14, and 16.5 Å.
The lid opening of BCL was reversed in simulations of 6 ns after changing the solvent from toluene to water, measured by distance Cα 138-Cα 250. The used starting conformations were selected from simulation of closed BCL in toluene after different times. The distance Cα 138-Cα 250 in the closed homology model was 6.1 Å.
In the crystal structures of BCL and BGL, the carboxylic group of the side chain of Asp130, located in the loop between helix α4 and α5, is coordinated by hydrogen bonds between the backbone and the side chain of Thr132, and the backbone of Ser135, stabilizing the conformation of the loop. During the simulations of open and closed BCL in water, the side chain of Asp130 was also coordinated by the backbone and the side chain of Thr132, and the backbone of Ser135, but these hydrogen bonds were partially lost during the simulation and replaced by hydrogen bonds to water molecules of the solvent. However, during simulations of closed BCL in toluene, Asp130 formed additional hydrogen bonds during lid opening and became fourfold coordinated by the backbones and side chains of Thr132 and Ser135. Furthermore, in the simulations of open BCL in toluene, Asp130 was sixfold coordinated forming two additional hydrogen bonds to backbone and side chain of Thr136 (figure 11). Thus, in toluene the loop between helix α4 and α5 was stabilized in the open conformation by the coordination of Asp130 in an extended hydrogen bonding to other amino acids of the loop.
Stabilization of Asp130 by hydrogen bonds. After the simulation of BCL in toluene Asp130 in the lid was coordinated by six hydrogen bonds to backbone and side chains of Thr132, Ser135 and Thr136. The secondary structure of BCL is colored grey, hydrogen, carbon, nitrogen and oxygen atoms are colored white, green, blue and red, respectively.
The interfacial activation of lipases is associated with a conformational change of the lid [11, 37]. The detailed analysis of the pathway of the conformational transition is not accessible in experiment. To get insight into the interfacial activation of BCL, multiple molecular dynamics simulations of the open and closed conformation of BCL in explicit solvent models of water and toluene were carried out without using restraints or external forces. An implicit organic solvent model was not used, because essential water molecules are supposed to be important to retain the flexibility of the lipase. Reproducibility of the observed properties was confirmed by performing three simulations for each system. The primary purpose was to apply molecular dynamics simulations examine the motion and conformational transition of the lid (residues 118–150) and the β-hairpin (residues 214–228) of BCL, which is not yet accessible to an experimental investigation.
For each system, a similar behaviour was observed: a fast opening of the lid in toluene starting with the closed structure, a closing of the open structure in water, and no major conformational changes in the simulation of the closed and open structure in water and toluene, respectively. Our major observations, the solvent-dependent opening and closing of the lid and the decoupling of the motions of lid and β-hairpin, were confirmed in an independent work in the group of P. Monsan (INSA, Toulouse) on simulation of conformational transitions of BCL: while lid opening occured at a water-hexane interface, closing of the lid was observed in water (I. André, personal communication).
In simulations of closed BCL in water, the lid stayed in its closed conformation. A slight further lid closing was observed which indicates that the homology model of closed BCL might not represent the closed conformation in solution. Furthermore, the lid showed a high conformational mobility in the absence of an oil-water interface which is supported by experimental observations. High B-factors of the lid were observed in all lipases in closed conformation [38–40], which led initially to the hypothesis that the lid of BGL can undergo a conformational transition. In crystallographic studies of closed Thermomyces lanuginosa lipase (TLL) in water, the lid was disordered , and in Rhizopus delemar lipase two different conformations of the closed lid were observed .
In simulations of open BCL in toluene, the lid further opened. This was also observed in Brownian dynamics simulations of Rhizomucor miehei lipase (RML) . At a lipid binding zone, which is comparable to a non-polar solvent, the lid further opened starting from the open crystal structure . The further lid opening might be due to a different stabilization of the open structure in non-polar solvents as compared to the crystal structure. While in non-polar solvents, the lid is stabilized by an increase of hydrophobic surface, the conformation of the lid in the crystal is the result of energetic compromises to form stable contact interactions . Upon molecular dynamics simulations of monomers in solution, starting with crystal structures, the structure is released from its crystal contacts and relaxed to a conformation close to that in solution . The overall flexibility in simulations of open BCL in toluene was about half the flexibility of closed BCL in water, which is in agreement with a general observation of a decreased flexibility of proteins in non-polar solvents in experiment [46, 47] and in molecular dynamics simulations [26, 48–51].
In our simulations of closed BCL in toluene, the lid opening by 18 Å was observed by a rigid-body movement of helix α5 without unfolding of helices α4 and α5. A similar rigid-body hinge-type motion of a single helix was also concluded from the existence of a closed and open crystal structure of RML . The lid opening of RML was observed in a low-dielectric medium, whereas in a high-dielectric medium no opening was observed . In our simulations the hydrophobic surface of BCL increased upon lid opening, which is in agreement with a general observation of most lipases, where lid opening is associated with an increase in hydrophobic surface [12, 20, 52, 53].
Previously, a partial opening of the lid has been investigated in simulations for different lipases. In molecular dynamics simulations in a continuum with different dielectric constants, lid opening was enhanced in a medium with a low dielectric constant, while the opening time of the lid increased for media with increasing dielectric constants . In previous Brownian dynamics simulations, the lid of RML opened during 100 ns in a low-dielectric medium, while in a high-dielectric medium the lid stayed in its closed conformation for 900 ns . In a 1 ns molecular dynamics simulation of RML in explicit water, the lid was highly flexible and a lid opening was concluded from essential dynamics analysis . The partial lid opening was also observed for RML , Humicola lanuginosa lipase (HLL) , and Candida rugosa lipase (CRL)  in explicit solvents. In short molecular dynamics simulations of open BCL in water and vacuum, no conformational transition of the lid and a similar behaviour in different solvent environments was observed . It was suggested that lid opening of HLL is a multi-step process involving more than two conformational transitions before a fully activated conformation is assumed . This is in agreement with our simulations of BCL, where a barrier was identified, blocking the movement of helix α5 by the N-cap of helix α6. While the generated homology model of closed BCL and the template of closed BGL show a long helix α6 (residues 156 to 166), helix α6 is shorter in the open structure of BCL (residues 160 to 166), where Asp157 is replaced by Asn in the sequence of BCL. Thus, the unfolding of the N-cap of helix α6 (residues 156 to 159) would be necessary to make the complete movement of the lid towards the fully open structure feasible. However, this unfolding was not observed in the time scale in our simulations of 30 ns. The blocking of helix α5 by helix α6 seems to result from a different secondary structure of helix α6 in the open and closed structure.
A correlation of the lid movement with a surface loop was previously observed in restrained simulations of Pseudomonas aeruginosa lipase, which was suggested to trigger the lid opening . In all our simulations of closed and open BCL in water, the β-hairpin drifted away from the lid, while it did not move in toluene, independent of the conformation of the lid. The conformational transition of the lid of BCL was not coupled to the β-hairpin or other surface loops, which was also not observed for other lipases [28, 30, 43, 55].
Different mechanisms of interfacial activation have been already proposed. While in the 'substrate theory', changes in the conformation of the lid are dependent on a bound substrate molecule [18, 19], in the 'enzyme theory' conformational changes on the enzyme are based on the adsorption to a lipid interface . The lid opening in our simulations was only driven by the hydrophobicity of the solvent, where a hydrophobic solvent favored the opening of the lid, which supports the 'enzyme theory' and experimental observations. However, the solvent might not be the only reason leading to a complete opening of the lid, and we cannot exclude a possible influence of a substrate intermediate covalently bound to the catalytic serine. Several lipases have been crystallized in an open conformation in the absence of a bound inhibitor [57, 14, 36]. The lid opening of Human pancreatic lipase by water-miscible organic solvents without a bound substrate was also observed in experiment using antibodies , and a hydrophobic patch led to a conformational transition to the open conformation of CRL .
The open conformation of BCL in water showed a partial lid closing during the simulations. However, lid closing in water was much slower than lid opening in toluene, and a complete movement of the lid to the closed conformation of the homology model was not observed. For CRL it was observed in experiment that the conversion between the open and closed conformation was very slow in aqueous solution in the absence of interfaces, which made the separation of the two conformations possible, while the exposure of CRL to a hydrophobic patch accelerated the transition . However, a transition state between the closed and the open conformation could not be isolated. Short molecular dynamics simulations of the open conformation of BCL in water and vacuum demonstrated the high flexibility of the lid and the β-hairpin . It was concluded from its high flexibility that the open structure of BCL becomes unstable in water leading to lid closing, however, a conformational transition from the open to the closed conformation was not observed.
The conformational transition of BCL from the closed to the open conformation of the lid in toluene could be reversed after changing the solvent from toluene to water. The analysis of eight simulations starting with intermediate positions of lid opening in toluene indicated that there are at least three local energy minima in addition to the closed crystal structure. In one simulation the lid closed completely, while in all other simulations a partially closing was observed. In contrast to the lid opening in non-polar solvents, the lid closing in water was a stepwise rather than a continuous process, associated with a partial unfolding and deformation of the helical structures in the lid.
The solvent was the driving force of the opening and closing of the lid. Local unfolding by breaking hydrogen bonds was mediated by water molecules, while the formation of hydrogen bonds was driven by the non-polar solvent. The formation of a local hydrogen bond network was most prominent in the loop between helix α4 and helix α5, which seems to direct the conformational transition. Asp 130 plays a pivotal role in the hydrogen bond formation and stabilizes the open conformation of the lid in toluene. While Asp130 was sixfold coordinated by backbone and side chain atoms after simulation in toluene, which was closely related to the movement of the loop, these hydrogen bonds were lost in water by coordination of water molecules of the solvent, leading to a destabilization of the open structure. A pivotal role of single amino acids directing the lid opening might not be restricted to BCL, as observed in previous simulations of TLL, where a solvent-dependent switch of Arg84 in the lid was observed .
The observed conformational transitions of the lid were dependent on the solvent. In simulations of closed BCL in water, no significant conformational change was observed, while in simulations of closed BCL in toluene the lid gradually opened. In simulations of open BCL in toluene, the lid opened slightly more than in the crystal structure, while in simulations of open BCL in water a partial closing of the lid was observed. In simulations of closed and open BCL in water, the hydrophobic β-hairpin moved away from the lid, while it showed no directed movement in simulations in toluene. Thus, the movement of the β-hairpin was independent of the movement of the lid.
The crystal structure of open BCL was taken from the Protein Data Bank [PDB: 3LIP]  with a resolution of 2.0 Å by X-ray diffraction as initial structure for the simulations. There was no crystal structure of the closed conformation of BCL available. A homology model of closed BCL was built by the protein modeling server SWISS-MODEL  using the closed conformation of the homologous lipase from Burkholderia glumae (BGL) [PDB: 1QGE]  as template.
pKa values and protonation states of titratable sites Arg, Lys, Asp, Glu and His at pH 7 were calculated using TITRA , based on the Tanford-Kirkwood model , using standard parameters. The solvent accessible surface area (SASA) of each residue was calculated by the program acc_run . In toluene BCL was protonated assuming pH memory from the protonation states in water [49, 63]. The electrostatic potential at pH 7 was calculated using DELPHI V. 4  with a dielectric constant of the solvent of 80 and a molecule interior of 4. Atomic charges and radii were taken from the PARSE charge and radii files .
Simulations were set up in XLEAP of the Amber 7.0 program package. Hydrogens were added as calculated by TITRA, His was protonated at Hδ-position. Disulfide bridges were built from information in the crystal structure. The BCL structure, including 193 crystal water molecules, was solvated using the explicit TIP3 water model (dielectric constant 78.5)  and a non-polar solvent model of toluene (dielectric constant 2.4)  in a truncated octahedral box with a minimal distance of 14 Å between the box boundary and the protein. Three Na+-ions were added in XLEAP as counter ions to neutralize BCL for simulations.
Multiple molecular dynamics simulations of the protein-solvent systems were performed using the AMBER 7 program package . The all-atom AMBER force-field ff99  was used to present the protein system and Ca2+-ions. The simulations were done in a truncated octahedral box under periodic boundary conditions. The Sander tool of AMBER 7 was used for minimization and simulations. Non-bonded interactions were calculated using the Particle-Mesh Ewald method to a cutoff distance of 10 Å and the SHAKE algorithm  was applied to constrain all bonds involving hydrogen atoms. The initial structures were energy minimized by applying 500 steps steepest descent and 50 steps conjugate gradient to relax clashes in the system. After the minimization steps the temperature was set to 300 K and the pressure to 1 bar under restrained conditions using a harmonic potential for all backbone atoms C, O and CA. The force constants were gradually decreased every 50 ps steps from 10, 5, 1 to 0.1 kcal/mol force constant, followed by a non-restrained simulation without additional external forces under periodic boundary conditions. Simulations were performed at 300 K using a time step of 1 fs. Temperature and pressure of the system were controlled using a weak coupling to an external heat bath  with a temperature coupling constant of 1.0 and a pressure coupling constant of 1.2. Three simulations, one up to 30 ns and two up to 15 ns, for the open and closed system in water and toluene were carried out using different starting atomic velocities from a Maxwell distribution to sample the conformational space. Each distribution was generated by a random number generator. The resulting trajectories were analyzed using PTRAJ of AMBER 7 after fitting the backbone atoms of the core (except residues 118–150 and residues 214–228) of each conformer to the initial structure. In PTRAJ the root-mean squared deviation (RMSD) of the backbone atoms between each conformer and the initial structure and between all conformers (2D-RMSD), atomic positional fluctuations relating to B-factors, and atom-atom distances were calculated.
Crystals were built up using SWISS-PDB Viewer and crystal contacts were analyzed by the WHAT IF web interface , including a 5.0 Å shell of symmetry related residues around the molecule, pairs of atoms were analyzed only between different asymmetric units. Secondary structure elements and the solvent accessible surface area (SASA) using a probe radius of 1.4 Å were calculated by DSSP . Protein structures were visualized using PyMol 0.98  and VMD . Electrostatic potentials and hydrophobicity, using the hydrophobicity scale of Eisenberg , were mapped on the surface in PyMol 0.98. The quality of the homology model was analyzed using the ProSA-web interface .
The work was carried out in the framework of the Sonderforschungsbereich 716 funded by the Deutsche Forschungsgemeinschaft (DFG).
PT carried out the simulations, RDS contributed to the discussion of the results, JP was the principal investigator and directed the research. All authors read and approved the final manuscript.


Works Here: Great teachers and academics. They are by far the best charter school in buffalo and really strive to help their students understand real world problems. Not only do they do their normal academics, but they teach the student things like how to manage money, right a check, get involved in your community, and being a responsible citizen! This schools academics is vigorous, but they still know how to let the kids have fun!


text:
29 Search Results for "Botswana" …
Search our video library for "Botswana"
Botswana Workshop Focuses on Military Curricula
In February 2018, the Africa Center for Strategic Studies held a curriculum development workshop for the State Department's Africa Military Education Program (AMEP) in Gaborone, Botswana. During the four-day event, participants from nine countries shared experiences, analyze sound practices, and discussed approaches to designing case studies that could be used in professional military education. Plenary... Continue Reading
AMEP Reference Materials
The Africa Military Education Program (AMEP) helps to strengthen professional military education institutions across the African continent through focused investments in faculty development and improved curriculum design and content.
Reshaping African Agency in China-Africa Relations
Spotlight published by Paul Nantulya on March 2, 2021
The power imbalance between China and Africa poses a challenge for negotiating equitable investment deals. The interests of African citizens can be strengthened through agreements that are transparent, involve experts, and facilitate public engagement.
Reimagining the Security Sector in Sudan
An academic webinar series exploring the lessons learned of the roles of the security sector and national security strategy development during times of transition from military to civilian rule. The webinar series provided an opportunity to share evidence-based insights and experiences and their implications for Sudan during its challenging transition to a civilian-led, democratic government.
Analyzing Africa's Second Wave of COVID-19
Infographic published by the Africa Center for Strategic Studies on January 5, 2021
2020 saw COVID-19 infect over 2.7 million Africans and kill over 65,000. A surge of cases in the last quarter of the year, combined with the emergence of more contagious mutations, pose new challenges for Africa in 2021.
The Spread of Surveillance Technology in Africa Stirs Security Concerns
Spotlight published by Bulelani Jili on December 11, 2020
The spread of surveillance technology in Africa without adequate checks and balances is reshaping the governance landscape while potentially enabling another tool of repression.
Mali Coup Offers Lessons in Democracy Building—but Junta Must Go
In defiance of a Sept. 15 deadline to step aside for a civilian transitional government set by the West Africa regional body, ECOWAS, Mali's coup leaders have proposed a plan that would keep the military in charge. A convenient provision of the plan is that leaders of the Aug. 18 coup would be granted judicial... Continue Reading
China Promotes Its Party-Army Model in Africa
Spotlight published by Paul Nantulya on July 28, 2020
China's party-army model, whereby the army is subordinate to a single ruling party, is antithetical to the multiparty democratic systems with an apolitical military accountable to elected leaders adopted by most African countries.
African Adaptations to the COVID-19 Response
Presidential task forces, staggered mobility, support for the most vulnerable, and local innovations mark Africa's adaptive response to the novel coronavirus pandemic.
What the Coronavirus Means for Africa
Spotlight published by Shannon Smith on February 4, 2020
Given its fragile public health systems and close ties to China, Africa is vulnerable to the spread of the coronavirus, highlighting the continent's centrality to global health security.
National Security Strategy Development Workshop: North and Eastern Africa
Program materials for the Africa Center's 2019 program, "National Security Strategy Development Workshop: Central and Southern Africa." Click here for syllabus, readings, and presentation slides.

redpajama_set_name: RedPajamaCommonCrawl


As Innoweave continues to support more organizations to access new tools and approaches to Social Innovation, it has become evident that a key factor to our success is our "community of coaches". Time and time again participants of the program have told us about the quality of the coaching they have received and how it has been essential to the success of the ongoing implementation of an approach in their organization.
Through the program's expansion, we are working with more individuals who have the skills and experience in a particular approach that Innoweave offers and who share a passion and commitment to building a stronger non for profit sector as partners with Innoweave.
As a registered coach with Innoweave, you will work with agency specific teams to help them implement an action oriented approach within their organization.
So, how do you become a coach, and what are the benefits?
First, it is important to understand the Innoweave process. As you will see from the graphic below, organizations will generally go through a 5 step process towards implementing a particular approach.
After reviewing information through our website and webinars, and taking an online self-assessment, organizations attend a workshop in particular approach. In these workshops teams from participating organizations develop actionable next steps to implement an approach. For example, a team coming out of a Social Enterprise workshop would have developed a draft feasibility study and business plan, and a team who had participated in the Constructive Engagement workshop would have the beginnings of an engagement plan.
We then ask organizations to connect with a Innoweave coach from our online database of registered coaches, select someone who fits their needs, and then develop a plan to build off the work the organization has begun to develop in the workshop. Organizations select a coach by reviewing the online database of coaches, undertaking due diligence to determine the suitability and fit of the coach with the goals of their organization (often phone/in-person interviews), and indicating on their application for an Innoweave Implementation Grant which coach they would prefer. Once organizations have identified a coach they would like to work with and decided upon the terms of their working arrangements, they can then apply for an Innoweave Implementation Grant designed to subsidize the cost of the coach.
We are looking for consultants, entrepreneurs, content experts, and sector leaders with the knowledge and skills to help work with interested community sector organizations to implement a specific tool or approach currently offered by Innoweave. These include, Collective Impact, Scaling Impact, Social Enterprise, Social Finance, Outcomes Finance, Developmental Evaluation, Cloud Computing, Constructive Engagement and Impact & Strategic Clarity .
How do I register to become a coach?
To register to become a coach, you can click here to be directed to our online registry where you will be asked to provide a short bio outlining your experience and expertise in a particular approach, your experience working and coaching community sector organizations (including listing organizations you have worked with in the past), and the geographic area you are interested in serving.
Once you have provided Innoweave with the information above, you will be listed on our database from which organizations can select you to become a coach.
What is the benefit to becoming an Innoweave coach?
More and more organizations are seeing the inherent value in the process developed by Innoweave. We are a platform for organizations who are ready to implement new approaches and increase their impact, and for consultants, entrepreneurs, content experts, and sector leaders who want to help them achieve their goals. Our process connects these two groups and supports them with Innoweave Implementation Grants.
Becoming an Innoweave coach also connects you with the growing number of other leaders working in this sector, and provides forums and tools for sharing and developing strong communities of practice.
If you have an interest in becoming an Innoweave Coach, please visit our website at Innoweave.ca and register by clicking here.
* Please note, the process for becoming a Impact & Strategic Clarity coach does not follow the same process as the other modules. For more information, you can email us at info@innoweave.ca.


Despite its critical nature, explosion proof lighting is quite often wholly misunderstood both in its basic nature and varying types. Tell someone their location requires an explosion proof light fixture and the first thing they'll likely assume is you mean a light that cannot explode. There is even more often a misunderstanding regarding the various types of safety lighting available and a lot of mistaken assumption that one type is interchangeable with another. For instance, some may assume that because a fixture is vapor proof it is safe to use in areas where flammable or explosive vapors are present, and thus is comparable to an explosion proof fixture. Nothing could be further from the truth, and such misunderstandings can lead to serious injury or even death.
Explosion proof lights are lamps and fixtures that have been designed specifically for use in areas where dangerous flammable, explosive or otherwise volatile gases, vapor, liquids and materials are or may be present. Locations such as these are considered "Hazardous Locations" and are defined by different codes and directives such as the NEC (National Electrical Code-USA), ATEX (European Union), CEC (Canadian Electrical Code) and similar codes and regulations. Such locations can have materials such as petrochemicals, explosive dusts, solvents and fibers which are present as a part of everyday operations or could be present under unusual conditions such as a container or pipeline leak. Regardless of when these locations have flammable or explosive materials present however, the electrical equipment used in locations classified as hazardous must comply with regulations and laws based on electrical codes regarding hazardous locations.
At the basic level, explosion proof lighting is equipment designed to prevent the ignition of flammable or explosive materials, gases, or vapors. Lighting is one of the most commonly encountered electrical devices in any type of workplace and the types of lighting used can range from high power permanent fixtures to a common flashlight used for portable illumination. Every type of light used in a hazardous location must be explosion proof certified regardless of its size or type. Since lighting equipment operates on electrical current, and electrical current can create heat or sparks, it must be properly designed specifically for use in hazardous locations if flammable or explosive materials may be present. Lighting can present an ignition danger in several ways, including but not limited to; the operating heat of the lamp, the minute sparks created by on/off switches, defective wiring or internal components which can lead to short circuiting, or heat buildup from the accumulation of dusts or fibers on the fixture. As a result, the manner in which lighting equipment meets regulatory compliance for hazardous locations can vary and is usually reflected by its design and the type of approvals it carries.
Lighting for hazardous locations must be certified explosion proof or intrinsically safe by an authorized third party testing organization such as Underwriters Laboratories which tests and certifies equipment according to the relevant electrical codes set out by the NEC, ATEX etc. Intrinsically safe and explosion proof certification is similar, however the two terms denote different levels of design which reflect how they protect against ignition. Explosion proof equipment is designed to withstand and contain the ignition of flammable materials within the fixture itself, whereas intrinsically safe equipment does not produce or carry enough electrical current to cause ignition. For all intents and purposes, intrinsically safe lighting represents the highest level of safety, while explosion proof lighting meets minimum requirements for a much wider variety of environments. Intrinsically safe lighting tends to be small, low powered, and impractical for general lighting applications, and so is much less common than explosion proof lighting which generally encompasses more powerful fixtures.
Explosion proof lights do not prevent ignition completely, but rather control it and prevent the atmosphere outside of the light fixture from igniting. This is accomplished in a few different ways, but the general premise is to contain an ignition within the lamp housing long enough for the ignited gases to cool before escaping from the fixture. Explosion proof lights are generally constructed of heavy gauge, thick walled metals such as aluminum for rigidity and strength. The joints are typically fitted together with fine threads which serve a dual purpose; they provide a strong joint that can withstand an internal explosion, and they actually allow the pressures created by an internal explosion to escape. They do this safely by forcing the escaping heated gases to slow down to the point that by the time they exit the fixture, they have cooled enough to be unable to ignite the atmosphere outside the light fixture.
So as can be seen, it is not that explosion proof lights cannot explode, but rather they can withstand and contain an explosion or ignition within themselves. In addition to being certified explosion proof, lighting for hazardous locations must also be approved for use around the different types of conditions and materials they might come into contact with. Hazardous locations are rated according to the likelihood of the hazardous condition, and the types of materials which make the area dangerous. Thus, locations are defined as Class 1 which refers to Gases or Vapors, or Class 2 which denotes combustible or electrically conductive dusts. Additionally, locations are further sub categorized according to the likelihood of the hazardous condition existing, with Division 1 denoting the presence of hazardous materials under normal conditions, and Division 2 denoting their presence under abnormal conditions such as a container leak. Locations are also broken down according to the types of materials and classified as Groups A through G. For a detailed description of hazardous location classification refer to our article "IECex/ATEX and North American NEC HAZLOC Equipment Classification".
To be suitable for a given hazardous location, a fixture must be certified according to Class, Divison, and Group. Thus, a Class 1 Division 1 Group C locations requires equipment carrying Class 1 Division 1 Group C certification. If the fixture does not carry this certification, it is not suitable for use in hazardous locations regardless of any manufacturer claims as to it being explosion proof.


Another season for the boys to head to Coll. Once again running along side Basking Shark Scotland. Cameron is up around Coll and getting some amazing interactions with the big fish. Struan has been up for a few days to help increase capacity. The sunny days and shallow sands have allowed for some exceptional photos. Lots of feeding and breaching have been spotted too.


When you install Oracle Enterprise Manager 11gR1 Grid Control an agent for mass deployment is included with the install. This mass deploy agent is for hosts that have the same OS in which Grid Control was installed. If you want the ability to deploy agents to hosts running other OSs you will need to download and install the mass deployment agent for that particular OS.
This document will detail adding the 32bit agent for Windows to an existing Enterprise Manager 11gR1 Grid Control install on 32bit Linux.
At the time of this writing only the 10.2.0.5 agent existed for Windows 32bit so I downloaded the file Win32_Grid_Control_agent_download_10_2_0_5_0.zip.
Oracle Enterprise Manager 11gR1 Grid Control uses the OMS_HOME/sysman/agent_download as the staging directory for agent mass deployment. Agents are placed in directories according to their version number. In our case the version is 10.2.0.5.0 so we will need to create 10.2.0.5.0 directory in OMS_HOME/sysman/agent_download.
After making the directory change into it, copy the agent to the directory and unzip it.
[oracle@gc 10.2.0.5.0]$ cp ~/Win32_Grid_Control_agent_download_10_2_0_5_0.zip .
That is it. The 32bit agent for Windows has been installed and is ready to deploy.
In Oracle Enterprise Manager 11gR1 Grid Control click on the Deployments tab.
On the Deployments page, scroll down to the Agent Installation section and click on the Install Agent link.
On the Agent Deployment type page click on the Fresh Install link on the upper left of the page.
On the Installation Details page, scroll down to the Version section. You should now see that 10.2.0.5.0 appears in the drop down.
When you select 10.2.0.5.0 you should see that in the Hosts section the platform changes Microsoft Windows (32-bit).
That is all there is to it. If you would like to see how to actually push the agent see the post: Setup Agent for Mass Deployment in Oracle Enterprise Manager 11gR1 Grid Control.
I will be ptuitng this dazzling insight to good use in no time.


Send SMS all around the world with 200+ countries available!
Your sender must have been authorized and respect the sms_sender format.
The default behaviour is to send your SMS with GSM 7-bit encoding. However, if your text contains a character that is not in the GSM 7-bit charset (Basic Character Set), we will send it as 16-bit UCS-2 (UNICODE) - using 2 bytes per character.
You can however force the encoding to be used at any time, using the force_encoding property.
If you force a GSM encoding, we will try to convert non-GSM characters to GSM ones. « becomes ", € becomes e, etc. The full mapping is available when calling the method sms.get_gsm_charset_mapping.
Please note that whatever the encoding forced or used, you always send your text as a JSON string to our API, without any special processing. The charset is applied in our platform before sending to the carriers.
We automatically handle concatenated SMS. The number of SMS parts billed will be set on the parts property of the SMS object. The object can be sent to you using Webhooks.
If it's equal to or less than 160 characters, it counts as 1 SMS.
If it's more than 160 characters, the split is done every 153 characters.
If it's equal to or less than 70 characeters, it counts as 1 SMS.
If it's more than 70 characters, the split is done every 67 characters.
$text = 'Some super mega ultra long text to test message longer than 160 characters '.
'Some super mega ultra long text to test message longer than 160 characters '.
Please note that limitations apply and vary from country to country when using SMS for marketing purposes.
Please refer to regulations in the countries you are targeting.
To receive DLR notifications, you can use Webhooks. You need to subscribe to the webhook sms.mt.status_update.
You're all set! DLR will be sent to this Webhook.
To receive DLR notifications, you can subscribe globally to the webhook sms.mt.status_update (like above). You can also use a "dynamic" webhook like below. DLR will be sent to both the global Webhook and the dynamic Webhook. Replies to this MT will also be sent to this specific Webhook.


text:
package operations;

import javax.swing.JOptionPane;

import data.Collector;
import graph.implementation.Graph;
import layouter.Layouter;

public class O_CompleteLayout implements Operation {

	private Layouter layouter;

	public O_CompleteLayout(Layouter layouter) {
		this.layouter = layouter;
	}

	@Override
	public void run() {
		Collector.getSlides().addUndo();
		Graph graph = Collector.getGraph();
		Graph next = layouter.getCompleteLayoutedGraph(graph);
		new O_RelaxAllEdges(next).run();
		Collector.getSlides().setSelectedGraph(next);
		Collector.getWindow().repaintBoard();

		if(next == graph) {
			JOptionPane.showMessageDialog(null, "Cannot layout this graph.");
		}
	}
}

redpajama_set_name: RedPajamaGithub


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Mamaearth is an online store which offers natural, toxin-free baby products such as lotions, oils, insect repellents and more.
You can still earn Cashback on your shopping at Mama Earth from IndianCashback.
There is NO Cashback on Mama Earth Mobile App.


September 28, 2013 was the date when the Maroon Monsoon hit Tempe for a big-time, Saturday night, Pac-12 South match-up with the University of Southern California Trojans. The Arizona State Sun Devils took a 20-14 lead into the half, but the Trojans marched down the field (three plays for 75 yards in 46 seconds) scoring a touchdown and regaining the lead 21-20 to start the third quarter. The Sun Devils counter-punched 15 seconds later on a 74 yard touchdown reception by DJ Foster to re-take the lead 27-21. Then, our "The ASU Devils Den Holiday Party 12 Pack of Plays" Play #2 happened which was a knockout blow to the Trojans and Lane Kiffen's head coaching career at USC.
Alden Darby intercepted Trojan quarterback Cody Kessler, and Darby returned it 46 yards for a Sun Devil touchdown.
Kiffen called play-action to challenge the Sun Devil safeties. Kessler made an okay hand-off fake and was looking at his two options to the boundary side of the field. A Trojan wide receiver was what could be a deep post, and the Trojans were hoping that Darby would double him, but Irabor played physically and stayed on the receiver. Darby read the tight end route by Xavier Grimble to the sideline, made a quick break on the ball, and returned it 46 yards, tip-toeing down the sideline in front of the Student Section for the Sun Devil touchdown.
The Sun Devils scored four more touchdowns after the Darby interception to defeat the Trojans 62-41. Later that evening, Kiffen was fired from USC, and Arizona State sat on top of the Pac-12 South standings. A position the Sun Devils would never relinquish during the 2013 season.
The catalyst for the victory over USC was Darby's big play interception return for a touchdown that sucked the life out of the Trojans, and that is why it is Play #2 of our "Holiday 12 Pack". Darby, the starting senior safety from Long Beach Millikan High, has a history of stepping up against USC. During the 2012 game in the Coliseum, Darby returned a Matt Barkley pass for a 70 yards interception touchdown, but that was in a Sun Devil loss. Certainly, this "pick 6" felt much better with the victory!
Our special thanks go out to JediASU for all of his long hours of hard work in creating these amazing YouTube clips for Sun Devil nation!
It was brought to my attention on 12/13/13 that another site covering Arizona State athletics has produced a blog series "ASU's 12 Plays of Christmas" previously. I came up with the idea for our series as I was reading Christmas stories and songs to my baby girl in the days following the Territorial Cup game. I had been keeping a running list of plays of the season, reached a total of 12 to 15 plays I considered top plays, and the term just came to me. However, I failed to do a proper check to ensure it hadn't been done before.
I will continue to write our series, but I will rename it. Since we have a podcast segment called "Beers of the Week" and since not everybody celebrates "Christmas", I have decided to rename the series "The ASU Devils Den Holiday Party 12 Pack of Plays", the 2013 edition.
We take great pride in providing Sun Devil nation the most Sun Devil information with the best independent, original, honest, and non-biased commentary, and in absolutely no way was I attempting to use a blog title another site had done previously.


Although smocking seems intricate and complicated, it can be surprisingly simple. Smocking is a sewing technique that gathers fabric tightly in multiple horizontal sewing lines. When you smock fabric tightly in this fashion, you will need more fabric to sew garments. If you want to make a smocked sundress, you must determine how much fabric you will need to create the smocked sewing technique before you start your sewing project.
Measure the upper chest measurement of the person for whom you are making the sundress. This will be the length of smocked fabric you need to make the sundress.
Make a sample of smocking on a 6-inch square of fabric. Create the same smocking technique on the square of fabric that you will use on the sundress. This typically involves approximately six lines of smocking.
Measure the square of fabric along the smocked edge after you smock it. Expect that the smocked edge will be as much as one-half to two-thirds smaller than the unsmocked fabric.
Divide the measurement of the fabric before smocking by the measurement after smocking. Multiply this answer by the length of fabric you need to go around the top of the sundress. Add 1 inch for the seam allowance. This answer is the length of fabric required to make a smocked sundress. For example, if the measurement of your smocked sample is 3 inches, divide 6 by 3 to equal 2. Multiply 2 by 25 (the chest measurement for a sundress for a girl) and add 1 to get 51. You will need a 51-inch length of fabric (roughly 1.5 yards) to make a smocked sundress.


PRIOR LAKE, MINN – The Shakopee Mdewakanton Sioux Community (SMSC) Gaming Enterprise, responsible for both Mystic Lake Casino Hotel and Little Six Casino, today announced that Angela Heikes is its new president and CEO.
Heikes has spent most of her 22-year career helping two Minnesota tribes build on their gaming resort success. Over the past five years, most recently as chief operating officer of the Gaming Enterprise and previous to that as vice president of strategic planning and analysis, Heikes provided strategic planning and performance analysis to SMSC leadership.
Specifically, Heikes directed the SMSC's development of a master plan for the Gaming Enterprise and tribal community. She also led the SMSC's growing partnership with nearby Mall of America by leading the development of JW Marriott Minneapolis Mall of America, which is owned by Hotel Development LLC, an SMSC enterprise.
Prior to her work for the SMSC, Heikes worked for the Mille Lacs Band of Ojibwe, rising to the tribe's highest corporate post, overseeing Grand Casino Mille Lacs, Grand Casino Hinckley, and a number of smaller businesses. She also worked for Grand Casinos, Inc., opening casinos in Mississippi and Las Vegas.
Heikes is known by Minnesota lawmakers and industry insiders as a central and highly credible figure in protecting the state's Indian gaming industry in its first 25 years. A University of St. Thomas graduate, Heikes is also a 2015 "Women in Business" honoree of the Minneapolis/St. Paul Business Journal, one of Global Gaming Business's "25 to Watch," and a 2010 recipient of Finance and Commerce's "Top Women in Finance" award.
Heikes replaces longtime president and CEO Edward Stevenson, whose 40-year gaming career was highlighted by 20 years of leading the SMSC's casinos and helping develop them into the Midwest's largest tribal gaming operations. Stevenson was instrumental in defining and executing the leadership succession plan that led to Heikes' selection.
Stevenson will continue his association with the SMSC to formalize a long-term economic development plan as the Community's economic development officer.
The Shakopee Mdewakanton Sioux Community is a federally recognized, sovereign Indian tribe located southwest of Minneapolis/St. Paul. Making its top priority to be a good neighbor, the SMSC is one of the top 10 philanthropists in Minnesota and donates more to charity than any other Indian tribe in America. It also focuses on being a strong community partner and a leader in protecting and restoring natural resources. The SMSC's government, Gaming Enterprise, and various other enterprises are collectively the largest employer in Scott County.
Mystic Lake Casino Hotel, the premier gaming facility in the Midwest, continually creates new, fun and exciting entertainment experiences for its guests. Mystic Lake® offers gaming, three lively bars, exceptional dining at seven restaurants, headline performers, unique special events, and luxurious accommodations. It is located 25 minutes southwest of Minneapolis/St. Paul in Prior Lake.
Visit Mystic Lake in RiverSouth—Land of Big Fun! RiverSouth is a joint public-private collaboration promoting premier entertainment destinations just minutes south of Minneapolis. With four of Minnesota's biggest attractions just four miles apart, there's fun around every bend. Partners include Canterbury Park, Mystic Lake Casino Hotel, Valleyfair, the Renaissance Festival, Shakopee Mdewakanton Sioux Community, and the cities of Prior Lake and Shakopee.


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Exploring brain insulin resistance in adults with bipolar depression using extracellular vesicles of neuronal origin. Journal of psychiatric research Mansur, R. B., Delgado-Peraza, F. n., Subramaniapillai, M. n., Lee, Y. n., Iacobucci, M. n., Nasri, F. n., Rodrigues, N. n., Rosenblat, J. D., Brietzke, E. n., Cosgrove, V. E., Kramer, N. E., Suppes, T. n., Raison, C. L., Fagiolini, A. n., Rasgon, N. n., Chawla, S. n., Nogueras-Ortiz, C. n., Kapogiannis, D. n., McIntyre, R. S. 2020; 133: 82–92
Accumulating evidence suggests that disrupted insulin signaling is involved in bipolar disorder (BD) pathogenesis. Herein, we aimed to directly explore the potential role of neuronal insulin signaling using an innovative technique based on biomarkers derived from plasma extracellular vesicles enriched for neuronal origin (NEVs). We leveraged plasma samples from a randomized, double-blind, placebo-controlled, 12-week clinical trial evaluating infliximab as a treatment of bipolar depression. We isolated NEVs using immunoprecipitation against neuronal marker L1CAM from samples collected at baseline and weeks 2, 6 and 12 (endpoint) and measured NEV biomarkers using immunoassays. We assessed neuronal insulin signaling at its first node (IRS-1) and along the canonical (Akt, GSK-3ß, p70S6K) and alternative (ERK1/2, JNK and p38-MAPK) pathways. A subset of participants (n = 27) also underwent whole-brain magnetic resonance imaging (MRI) at baseline and endpoint. Pre-treatment, NEV biomarkers of insulin signaling were independently associated with cognitive function and MRI measures (i.e. hippocampal and ventromedial prefrontal cortex [vmPFC] volumes). In fact, the association between IRS-1 phosphorylation at serine site 312 (pS312-IRS-1), an indicator of insulin resistance, and cognitive dysfunction was mediated by vmPFC volume. In the longitudinal analysis, patients treated with infliximab, a tumor necrosis factor-alpha antagonist with known insulin sensitizing properties, compared to those treated with placebo, had augmented phosphorylation of proteins from the alternative pathway. Infliximab responders had significant increases in phosphorylated JNK levels, relative to infliximab non-responders and placebo responders. In addition, treatment with infliximab resulted in increase in MRI measures of brain volume; treatment-related changes in the dorsolateral prefrontal cortex volume were mediated by changes in biomarkers from the insulin alternative pathway. In conclusion, our findings support the idea that brain insulin signaling is a target for further mechanistic and therapeutic investigations.
View details for DOI 10.1016/j.jpsychires.2020.12.007


Coming off their second best appearance of the year the Women Eagles 7s will look to move up the table in Paris. The team currently sits in fifth place tied on 44 points with Canada. Russia are right behind with 43 points. If the U.S. can be better than both of those teams on the weekend they will nab a coveted top four spot and momentum heading into the 7s World Cup.
To reach that milestone head coach Richie Walker has once again chosen players with plenty of experience. Kristen Thomas is back after missing Langford due to injury. Quinnipiac standout Ilona Maher is also in the squad. They join Jordan Gray, Cheta Emba, Abby Gustaitis, Nana Fa'avesi, Ryan Carlyle, Nicole Heavirland, Kayla Canett, Lauren Doyle, Naya Tapper, and Alev Kelter.
The tournament kicks off on June 8th with the draw to be determined.


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Q: Correlation between " Time of the day" and an ordinal variable My hypothesis is  The compliance score (Dependent/ ordinal variable) varies during a different time of the day.
for example, I would expect high compliance between regular working hours 7 am - 5  pm -and lower scores between 5 PM and  7 am the next day.
I am not sure what test I should use.

A: If the dependent measure has multiple categories that you want treated as ordinal (like low, medium, and high compliance) then look at the PLUM procedure in IBM SPSS Statistics in the Base module.

redpajama_set_name: RedPajamaStackExchange


Canadian singer Leonard Cohen has died aged 82, according to a statement on his official Facebook page.
His career in music spanned almost five decades, and saw him inducted into the the Canadian Music Hall of Fame and the American Rock and Roll Hall of Fame.
During a promotional tour ahead of the release of his fourteenth studio LP, he confessed he was 'ready to die'.


In great condition with brand new tires. The retro styled cruiser offers the most satisfying ride for a wide range of enthusiasts, as well as a classic design with a power-packed V-twin engine that's just right for today's budget-minded consumer. The 2012 Honda Shadow Spirit 750 is a great blend of modern ingenuity and comfort. Weighing in at 536 pounds in running order, the 2012 Honda Shadow Spirit 750 comes equipped with a 745cc engine with a 3.7 gallon fuel capacity.


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Q: Always use _ instead of - on Woocommerce product attribute's slug Apparently Woocommerce seems to have the bad habit of changing the way over time it creates its slugs. Sometimes it puts all words together, sometimes uses _ and sometimes -, depending on the Woocommerce version.
This is creating me a huge problem since my shop is connected to an external warehouse software that connects both physical shop with woocommerce shop warehouse. Unfortunately, in order for the connection to work correctly, the attribute slugs must always use _ instead of -.
I wonder if there is some automatic way to do this? Perhaps some tweek I can do on the functions.php or some Woocommerce file I can edit? And if possible, how could I do that?
Many thanks in advance!

A: The product attribute taxonomy slugs begin all by pa_ (as product attribute).
Since a long time, if there is a white space (+ some other characters) they are replaced by a dash - and prohibited characters are removed. It's no more complicated than that.
For the connection to your external warehouse use in beetween str_replace() for the slugs conversions, this way:
// Here $taxonomy is the woocommerce product attribute slug
$right_slug = str_replace( array( 'pa_', '-' ), array( '', '_' ), $taxonomy );

It will:

*

*Remove pa_ from the begining (when it appear),

*Replace all - by _.

This should solve your problems.


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Ethiopia Food Security Outlook, December 2018
By Admin | January 2, 2019
Poor October to December seasonal rainfall and sustained ethnic clashes continue
Full Report in PDF
Deyr/Hagaya seasonal rainfall (October to December) in southern pastoral areas has been below average. It has been also erratic in temporal and spatial distribution and the onset was delayed. Southeastern pastoral areas continue to recover from drought in 2016 and 2017 and will remain in Crisis (IPC Phase 3) through at least May 2019.
Meher harvests are generally average throughout much of the country. Over parts of eastern Oromia, southern Tigray, eastern Amhara, and northern SNNPR, however, rainfall was below-average, leading to reduced production. Stressed (IPC Phase 2) and Crisis (IPC Phase 3) outcomes are expected in affected areas, as well as in many northern pastoral areas.
While the country continues to respond to the needs of drought affected populations, large populations are also displaced by conflict throughout the country. Areas where intercommunal clashes are having the most significant impact on food security outcomes include parts of Oromia, SNNPR, Somali, and Benishangul Gumuz regions.
Rainfall performance has been mixed over areas of southeastern and southern Ethiopia that typically receive Deyr/Hagaya rains between October and December. Seasonal rainfall started earlier than normal in the east of the Somali Region but was delayed by one to two weeks in most other areas. Moreover, the rainfall was significantly below average and erratically distributed across Somali region and southern pastoral areas of Oromia and SNNPR. Based on rainfall from October to 15 December 2018 and the NOAA/CPC forecast through December 31, wide areas southern pastoral areas of Ethiopia will accumulate large rainfall deficits (Figure 1).
Conditions for pasture and water in northern and southern pastoral areas area mixed. In southern pastoral areas, successive improvements in rainfall seasons had improved water and pasture conditions following droughts in 2016 and 2017. This in turn contributed to improved livestock body condition and conception rates and camels and goats are birthing again. Poor rainfall performance during the ongoing Deyr/Hagaya season, however, will limit the good recovery seen during previous months. In pastoral areas of Afar and northern Somali (Sitti and Fafan zones) regions, availability of pasture and water is expected to seasonably deteriorate during the dry season through March 2019.
Livestock prices are generally stable in most markets, improving compared to last year and average. According to field observations in Somali region and Borana zone of Oromia, livestock prices show an increasing trend. The price increases are associated with an improvement in livestock body conditions and low market supply as pastoralists are recovering from past droughts. As per Somali Region DPPB market data for Warder for the month of November, average locally consumed Goat price increased by 9, 23, and 54 percent, compared to last month, the same month last year, and the five years average respectively. Goat to maize terms of trade were up by about 25 percent compared to same month last year and the five years average.
On the other hand, livestock prices show a decreasing trend in the north of Afar region. For instance, the price of an average sized goat in November in Teru and Awera woredas declined by 38 and 14 percent, respectively, compared to the same month of last year. Livestock market supply is expected to increase in the upcoming long dry Jillal season due to livestock feed shortages and increased household purchase needs.
Following generally average Kiremt seasonal performance, Meher harvest prospects at the national level are expected to be near average. Unseasonal rainfall in October and November, however, did cause minor crop losses in major Meher crop producing areas of the country. The Meher assessment teams did also confirm localized areas of below-average production due to erratic rainfall, conflict, and pests during the main cultivation season.
Prices for locally produced staple foods have remained high since the start of the last lean. Prices are stable at elevated levels. For example, the price of sorghum in October in Boke woreda is 36 and 20 percent higher than October 2017 and the reference year, respectively. The wholesale maize price in Hosanna market increase by 9.3 percent compared to last month (October 2018), 6.4 percent compared to the same month last year, and 33.3 percent compared to the five-year average (Figure 2).
Conflict across different parts of the country continues to lead to displacement. According to IOM and partner reports, the number of conflict-related IDPs in 2018 alone could be as high as more than 1.5 million people across the country. The level of displacement is expected to increase as localized conflicts continue. For example, in the second week of December 2018, conflict along the Oromia-Somali border in Borena zone, specifically around Moyale, resulted in the displacement of thousands of people. In this clash, as per the report by Ethiopian News agency (ENA) on December 16, 2018, 21 people died, and 61 others injured.
Admissions for acute malnutrition treatment in Somali and Oromia regions remain high (Figure 3). The caseload for treatment of severe acute malnutrition in Oromia and Somali regions was approximately 112,956 and 72,144 admissions between January and October 2018 respectively, or approximately 66 percent of admissions in all of Ethiopia (280,892 children). A total of 11,340 and 6,673 admissions occurred in the month of October alone in Oromia and Somali regions respectively.
Across the country, total TFP admissions of malnourished children under 5 in October 2018 was 6.1 and 7.8 percent lower than September and July. The level of admissions was similar to the same month of last year but 8.3 percent higher than the five-year average.
For detailed projection click Full Report in PDF
Afaan Oromoo English
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