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Chemistry Tim Bugg Group
Peptidoglycan
Lignin Degradation
Carotenoid Cleavage Dioxygenases
Mhp Enzymes
Goran M. Rashid
Previous Group Members
Group Social Activities
Christmas Lunch 2016
Group Activities 2014
Bugg Group Christmas 2013
Previous Group Photos
Punting Trip 2007
DNA protocols
Cloning and transformation
Protein protocols
General Lab Techniques
Orange Experiment
Scientific writing guides
Phenylpropionate catabolic pathway
Enzymes of the Phenylpropionate Catabolic Pathway of Escherichia coli
The persistence in the environment of man-made chemicals, particularly chlorinated aromatics such as DDT and polychlorinated biphenyls (PCB's), in the form of pesticides and industrial chemicals is an issue of increasing public concern. By studying bacterial pathways involved in biodegradation of aromatic compounds, we seek to understand the enzymatic processes involved in their breakdown. We hope that a better understanding of the molecular basis for aromatic biodegradation will eventually lead to the design of improved biological catalysts for bio-remediation of chemical pollutants.
We are currently studying a catabolic pathway found in Escherichia coli responsible for the degradation of phenylpropionic acid, on which E. coli can grow as a sole carbon source. Oxidative ring cleavage is catalysed by 2,3-dihydroxyphenylpropionate 1,2-dioxygenase (MhpB), to give a yellow ring fission product which is cleaved by an unusual C-C hydrolase enzyme MhpC to give succinic acid and 2-hydroxypentadienoic acid. The latter unstable dienol is hydrated by a Mn2+-dependent hydratase enzyme MhpD to give 4-hydroxy-2-keto-pentanoic acid, which is the substrate for retro-aldol cleavage by aldolase MhpE.
Most of the research in the group has focused on extradiol dioxygenase MhpB and C-C hydrolase MhpC, however we have also examined the final two enzymes on the pathway, hydratase MhpD and alsolase MhpE.
1. 2,3-Dihydroxyphenylpropionate 1,2-dioxygenase (MhpB)
2,3-Dihydroxyphenylpropionate 1,2-dioxygenase (MhpB) is a non-heme iron (II) dependent extradiol dioxygenase, which has been overexpressed, purified and characterised [1]. Amino acid sequence alignments have revealed that this enzyme is a member of a distinct class of extradiol dioxygenases, containing a catechol 2,3-dioxygenase from Alcaligenes eutrophus, which we have also purified [2]. We have investigated the catalytic mechanism of MhpB using 18O2labelling experiments and synthesis of reaction intermediates. From these experiments we have obtained evidence in favour of a lactone intermediate in the mechanism, formed by a type of Criegee rearrangement [3].
We have also synthesised cyclopropyl-containing substrate analogues to act as radical traps for this enzyme, and we have observed a novel cis-trans isomerisation of the cyclopropyl ring during enzymatic processing, due to a reversible opening of the cyclopropyl ring. This provides evidence for a semiquinone radical intermediate in the enzyme mechanism [4].
We have synthesised carba- analogues of the two possible hydroperoxide intermediates, in order to identify which is the true intermediate in the MhpB reaction mechanism. The C-1 carba analogue (R=Me) showed no inhibition of MhpB, nor did the R=Me C-2 analogue. However, the R=tBu C-2 analogue, in which the hydroxymethyl substituent is held in an axial orientation, acts as a reversible competitive inhibitor for MhpB, consistent with the intermediacy of the C-2 hydroperoxide intermediate in the catalytic mechanism [5].
We have discovered a model reaction for extradiol catechol cleavage involving 1,4,7-triazacyclononane (TACN), FeCl2or FeCl3, pyridine (3 equiv) in methanol, which gives a good yield of muconic semialdehyde methyl ester. The reaction is highly selective for the macrocyclic ligand, which mimics the tridentate co-ordination chemistry observed in the extradiol dioxygenase active site. Interestingly, the FeCl2reaction shows higher extradiol/intradiol selectivity (7:1) than the FeCl3reaction (2:1), indicating that Fe(II) has an inherent chemical preference for extradiol cleavage, as found in the enzyme active site [6].
We have explored the mechanism of this reaction, which is the only iron (II) based model reaction to give a derivative of the true extradiol cleavage product. The reaction proceeds using the mono-sodium salt of catechol in the absence of pyridine, but not using the di-sodium salt, implying that catechol binds as its mono-anion. However, in this case the product distribution is very different, favouring intradiol cleavage by 15:1, implying that pyridine has an additional role, perhaps as a proton donor. Repeating the reaction with catechol mono-sodium salt in the presence of 1 equivalent of pyridine hydrochloride results in a switch back to extradiol cleavage, in a 4:1 ratio. These results suggest that the role of pyridine is two-fold: one equivalent is required as a base, but subsequently the protonated pyridinium salt acts as a proton donor, probably to catalyse the Creigee rearrangement step. These results provide some insight into the acid/base catalysis of the extradiol dioxygenases, and suggests roles for acid/base groups in the enzyme active site [7].
Two active site histidine residues, His-115 and His-179, were identified in MhpB that might act as acid-base catalytic residues. Replacement of either His residue by Gln by site-directed mutagenesis gave inactive mutant enzymes. Replacement of adjacent Asp-114 by Ala also gave an inactive mutant, however the D114N mutant retained a low level of activity. Analysis of the pH/rate profile of this latter mutant showed a loss of activity at high pH, indicating an effect on acid catalysis. Further studies indicate that His-115 is the catalytic base, while His-179 is an acidic group required for the final lactone hydrolysis step [8].
Recent studies have focussed on how the extradiol and intradiol catechol dioxygenase active sites catalyse two different Criegee rearrangements on a common hydroperoxide intermediates, as first discussed in 2001. Using error-prone PCR, we have selected 6 MhpB mutants of modified substrate specificity: two of these mutants were found to catalyse the formation of 5-15% intradiol product, consistent with the partitioning of a common intermediate [9]. We are currently using mechanistic probes to study the alkenyl and acyl migration mechanisms for Criegee rearrangement in the extradiol and intradiol catechol dioxygenases.
2. 2-Hydroxy-6-Keto-Nona-2,4-Diene 1,9-Dioic Acid 5,6-Hydrolase (MhpC)
The dienol ring fission product has been characterised and used to purify the hydrolase enzyme MhpC to near homogeneity. The identity of the MhpC products has been established, and by performing the enzymatic reaction in 2H2O the stereochemistry of the reaction has been established as proceeding with overall retention of regiochemistry [10]. Evidence for an MhpC-catalysed ketonisation of the dienol substrate has been obtained by 2H exchange experiments [11].
Pre-steady state kinetic analysis of the MhpC reaction has confirmed the existence of a discrete intermediate, and has revealed that approximately 50% of the keto-intermediate is released from the active site per catalytic cycle. A high Kdfor the substrate was measured (30 µM), although Km= 7 µM, suggesting that the substrate is bound in astrained non-planar conformation, thus promoting ketonisation [12].
Amino acid sequence alignments reveal that this family of C-C hydrolase enzymes is in the alpha/beta-hydrolase superfamily, containing a serine-histidine-aspartate catalytic triad, as found in the serine proteases. However, rapid quench studies using a synthetic radiolabelled substrate have yielded a very low yield of labelled protein, suggesting that there is no covalent acyl enzyme intermediate. Evidence in favour of a general base mechanism (involving base-catalysed attack of water on the ketonised substrate) has been obtained by incorporation of a small amount of two atoms of 18O from H218O. A non-hydrolysable substrate analogue, 4-keto-nona-1,9-dioic acid (KNDA) was found to act as a time-dependent inhibitor of MhpC, and was found to undergo
time-dependent incorporation of 18O from H218O into the ketone carbonyl, consistent with the formation of a gem-diol intermediate [13].
The crystal structure of E. coli MhpC has been determined, in collaboration with Prof. S. Wood (Dept. of Biochemistry, University of Southampton), in the presence of a non-cleavable analogue [14]. The catalytic Ser-110 is positioned very close to the carbonyl group of the substrate analogue, however the Ser-110/His-263 pair straddle the substrate in an arrangement different to that found in the serine proteases. Pre-steady state kinetic analysis of S110A and H263A mutants have shown that Ser-110 is not required for the initial keto-enol tautomerisation step, but is required for C-C cleavage; while His-263 is required for both tautomerisation and C-C cleavage [15]. Arg-188, positioned near the C-1 carboxylate group, is responsible for substrate binding, but also has a catalytic role in keto-enol tautomerisation, probably in substrate destabilisation [16].
We have developed a general synthetic route to the meta-ring cleavage products, using a palladium-mediated Heck coupling to synthesise the central diene. This route has been used to synthesise a series of substituted aryl-containing substrates for C-C hydrolase BphD, found on the biphenyl degradation pathway of Pseudomonas sp. LB400. A Hammett plot of log(kcat) versus sigma gave a reaction coefficient of –0.71 for C-C cleavage, consistent with a departing carbanion in the transition state of the enzyme catalysed reaction. Furthermore, a reduced substrate analogue containing a C-6 hydroxyl group was found to be a substrate for BphD-catalysed aldol-type cleavage, consistent with a general base mechanism [17]. Using this synthetic route, we have synthesised substrate containing a 13C label at C-6. Treatment of BphD with this labelled substrate gives a new NMR signal at 128 ppm, consistent with a gem-diol intermediate, with no appearance of an acyl enzyme intermediate at 170 ppm [18].
MhpC shares sequence similarity with a/b-hydrolases of diverse catalytic function: esterases, haloperoxidases, even cofactor-independent dioxygenases! In order to rationalise this diverse range of catalytic activities, we have suggested that these enzymes are able to activate a range of nucleophiles and diatomic substrates, including water, hydrogen peroxide, and dioxygen [19]. We have shown that MhpC and BphD both possess esterase activity, which has allowed a physical organic chemical study of esterase activity, by means of a Hammett plot [20]. We have recently shown that MhpC is also able to activate hydroxylamine as a nucleophile, and is able to catalyse C-C bond formation reactions in organic solvents [21].
3. 2-Hydroxypentadienoic Acid Hydratase (MhpD)
The ketonisation of 2-hydroxypentadienoic acid in aqueous solution has been studied and compared with its homologue enolpyruvic acid [22]. Hydratase MhpD is dependent on a Mn2+cofactor, which appears to be involved in substrate activation. The enzyme has been purified to homogeneity, and mechanistic studies undertaken [23]. The mechanism is thought to involve ketonisation of the substrate, followed by attack of a Mn2+-activated water.
4. 4-Hydroxy-2-Keto-Pentanoic Acid Aldolase (MhpE)
Aldolase MhpE catalyses the aldol condensation of acetaldehyde and pyruvic acid to give 4-hydroxy-2-keto-pentanoic acid. We have purified the enzyme 30-fold from Escherichia coli, and we have determined that the enzyme is a class 1 aldolase utilising an imine linkage with an active site lysine residue to activate the ketone of pyruvic acid for aldol reaction. The enzyme has been shown to catalyse the reverse reaction (i.e. C-C bond formation), but the equilibrium constant lies heavily in favour of C-C cleavage. The enzyme is selective for acetaldehyde as carbonyl acceptor, but is able to utilise a range of -keto acids as carbonyl donor [24]. This enzyme could therefore be amenable for use in selective C-C bond forming biotransformations.
[1] T.D.H. Bugg, Biochem. Biophys. Acta 1202, 258-264 (1993)
[2] E.L. Spence, M. Kawamukai, J. Sanvoisin, H. Braven and T.D.H. Bugg, J. Bacteriol., 178, 5249-5256 (1996)
[3] J. Sanvoisin, G.J. Langley & T.D.H. Bugg, J. Am. Chem. Soc. 117, 7836-7837 (1995)
[4] E.L. Spence, G.J. Langley, and T.D.H. Bugg, J. Am. Chem. Soc., 118, 8336-8343 (1996)
[5] C.J. Winfield, Z. Al-Mahrizy, M. Gravestock and T.D.H. Bugg, J. Chem. Soc. Perkin Trans. 1, 3277-3289 (2000)
[6] G. Lin, G. Reid, and T.D.H. Bugg, J. Chem. Soc. Chem. Commun., 1119-1120 (2000)
[7] G. Lin, G. Reid, and T.D.H. Bugg, J. Am. Chem. Soc., 123, 5030-5039 (2001)
[8] S. Mendel, A. Arndt, and T.D.H. Bugg, Biochemistry, 43, 13390-13396 (2004)
[9] T.D.H. Bugg and G. Lin, J. Chem. Soc. Chem. Commun., 941-952 (2001)
[10] W.W.Y. Lam & T.D.H. Bugg, Chem. Commun., 1163-4 (1994)
[11] W.W.Y. Lam & T.D.H. Bugg, Biochemistry, 36, 12242-12251 (1997)
[12] I.M.J. Henderson & T.D.H. Bugg, Biochemistry, 36, 12252-12258 (1997)
[13] S.M. Fleming, T.A. Robertson, G.J. Langley, and T.D.H. Bugg, Biochemistry, 39, 1522-1531 (2000)
[14] G. Dunn, M.G. Montgomery, F. Mohammed, A.Coker, J.B.Cooper, T. Robertson, J-L. Garcia, T.D.H. Bugg & S.P. Wood, J. Mol. Biol., 346, 253-265 (2005)
[15] C. Li, M.G. Montgomery, F. Mohammed, J-J. Li, S.P. Wood, and T.D.H. Bugg, J. Mol. Biol.,346, 241-251 (2005)
[16] C. Li, J-J.Li, M.G. Montgomery, S.P. Wood, and T.D.H. Bugg, Biochemistry, 45, 12470-12479 (2006)
[17] D.M. Speare, S.M. Fleming, M.N. Beckett, J-J. Li and T.D.H. Bugg, Org. Biomol. Chem., 2, 2942-2950 (2004)
[18] J-J. Li, C. Li, C.A. Blindauer, and T.D.H. Bugg,Biochemistry, 45, 12461-12469 (2006)
[19] T.D.H. Bugg, Bio-Organic Chemistry, 32, 367-375 (2004)
[20] J-J. Li and T.D.H. Bugg, Org. Biomol. Chem., 5, 507-513 (2007)
[21] C. Li, M. Hassler, and T.D.H. Bugg,ChemBioChem 9, 71-76 (2008)
[22] J.R. Pollard, I.M.J. Henderson, and T.D.H. Bugg, J. Chem. Soc. Chem. Commun., 1885-1886 (1997)
[23] J.R. Pollard & T.D.H. Bugg, Eur. J. Biochem., 251, 98-106 (1998)
[24] J.R. Pollard, D. Rialland, and T.D.H. Bugg, Appl. Environ. Microbiol.., 64, 4093-4094 (1998)
Telephone: +44 (0)24 76 523653
Undergraduates: +44 (0)2476 523678
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Graduate PhD enrolment: +44 (0)2476 522230
Department of Chemistry, University of Warwick, Gibbet Hill, Coventry, CV4 7AL
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Last revised: Fri 25 May 2012


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"It's Just A Dare" – Man After Sending Di*k Pic In Whatsapp !! Internet Thrashed Him
Female online users, especially those who are associated with media industry are being subjected to online harassment since the emergence of the digital world. Men and women across the social media platforms are protesting day in and day out against online harassment. However, the number of miscreants who find pleasure in sending inappropriate texts to women seems to have increasing in daily manner. Now, a journalist named Damini Srivasthava went through such trauma and unlike many women, she brought the matter to the light and caused a debate in the micro blogging social media site.
Women are regularly subject to online rape threats, online harassment, cyber stalking, blackmail, and more. As the internet becomes an increasingly important part of human existence and a critical space for marginalized populations to make their voices heard, a woman's inability to feel safe online is an impediment to her freedom, as well as to her basic human rights. Yet the problem of online violence and harassment is often overlooked in discussions of violence against women.
Damini Shrivasthava whose bio says that she is an editor in a media portal, captured the screen shots of the messages she received from a guy and vented out her emotions of how she felt while interacting with him in Whatsapp. The guy who seems to be a stranger, sent the picture of a penis to Damini and asked her to guess who he is.
When she was about to report him, the man in the other end pretends to be a known person of the victim and could be seen buying time from her to prevent himself getting blocked or reported. Later, he says that it is "just" a dare and wants Damini not to be mad at him.
Check out the screen shots shared by the journalist :
Sharing these screen shots, Damini shared what she felt while interacting with him by writing "Men really don't understand the horror/trauma one goes through because of this gratuitous behaviour, do they?" as her caption.
Check out her post below :
Men really don't understand the horror/trauma one goes through because of this gratuitous behaviour, do they? pic.twitter.com/bSVaJC5IAc
— Damini Shrivastava (@DammitDamini) February 2, 2021
This tweet went viral among the users of Twitter who are slamming the person who sent such insensitive messages. Damini confirmed that she has filed a police complaint against the person as she wants him to realize that what he did is not Okay.
Yes, I did. He needs to know this is NOT OKAY
She also confirmed that he is a complete stranger to her and his mobile number looked like it's from US.
I did. Right after I blocked. Some US number. No idea who/what/why does he have my number.
"This is illegal under both the IPC and the IT act. You can threaten legal action next time if that makes you feel more empowered. Otherwise, as others suggested, block." suggested a twitter user and many others reacted to get him punished by the law as well.
This is illegal under both the IPC and the IT act. You can threaten legal action next time if that makes you feel more empowered.
Otherwise, as others suggested, block.
Heinous sense of entitlement!!! And ick!
— Riddhiculous (@RiddhiAswani) February 2, 2021
I get so angry at this shit. Earlier a few of my male friends used to try this on phone: "guess who? Three guesses. I know you for a long time" at a time I was getting weird stalkerish calls. I used to simply hang up till they identified themselves
— Rituparna Chatterjee (@MasalaBai) February 2, 2021
If this was received on whatsapp as it seems by the screenshot, please approach the cops (as intimidating as that seems). Ppl who do this should not be spared.
— Saif (@bandrabachha) February 2, 2021
How dare that mf say "just a dare" as if it's a daring thing to do. Y'all shouldn't tolerate shit like this at all. Expose him to his parents already.
— 🔟™ (@highonmessi) February 2, 2021
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Free Picks » MLB Picks » Baltimore Orioles at Tampa Bay Rays 4-27-2016 Free MLB Picks & Predictions
Baltimore Orioles at Tampa Bay Rays 4-27-2016 Free MLB Picks & Predictions
Probable Pitchers: Chris Tillman vs. Matt Moore
The Baltimore Orioles visit Tropicana Field on Wednesday to play the Tampa Bay Rays. The probable starters are Chris Tillman for the Orioles and Matt Moore for the Rays. The opening line for this matchup has Baltimore at +120 and Tampa Bay at -130. The over/under was set at 7.5. The Orioles have a 6-11-1 over/under record and a 10-8-0 run line mark, meaning they cover 56% of the time. The Rays are 9-10-0 against the run line and have a 5-11-3 over/under record. They cover the spread 47% of the time.
The Orioles head into this matchup with a 11-7 record, including 4-6 on the road. Starting pitcher Chris Tillman has a 1-1 record with an earned run average of 4.42 and a WHIP of 1.26. He has 15 strikeouts over his 18.1 innings pitched and he has given up 17 hits so far this season. He has allowed 8.3 hits per 9 innings and he has a FIP of 3.3. The bullpen this year has an earned run average of 1.78 and they have given up 47 base hits on the year. Teams are hitting .201 against the bullpen while being struck out 61 times and walking 25 times this season. As a team, Baltimore has allowed 8.31 hits per nine innings while striking out 7.85 batters per nine. They are 12th in the league in team earned run average at 3.73. The Orioles pitchers have collectively given up 145 base hits and 65 earned runs. They have allowed 12 home runs this season and they allow 0.7 homers per nine innings as a staff. Baltimore as a pitching staff has walked 55 batters and struck out 137. They walk 3.2 men per 9 innings while striking out 7.9 per 9. They have a team WHIP of 1.27 and their FIP as a unit is 3.53.
As a team, Baltimore is batting .269, good for 5th in the league while putting together a .256 average away from home. The Orioles hold a .461 team slugging percentage and an on-base percentage of .330 which is good for 7th in baseball. They rank 8th in baseball with 9.06 hits per game. Chris Davis comes into this game hitting .215 and his on-base percentage is at .363. He has 14 hits this season along with 17 runs scored and 13 runs batted in. He's struck out 26 times and has walked 15 times. Manny Machado is hitting .360 and he has an on-base percentage of .415. He has totaled 27 hits so far while scoring 16 runs and he's driven in 11. He has walked 6 times and has struck out 15 times. The Orioles have 163 hits, including 36 doubles and 27 home runs. They've stolen 4 bases while they've been thrown out stealing 3 times. Baltimore has walked 55 times this season and they've struck out 152 times as a unit. They've left 116 men on base and have a team OPS of .792. They score 4.5 runs per contest and have scored a total of 81 runs so far this year.
Tampa Bay comes into this matchup with a 6-5 home record and a 9-10 overall mark. With an earned run average of 3.60, Matt Moore has a 1-1 record and a 1.12 WHIP. He has 26 strikeouts over the 25 innings he's pitched during which he has given up 23 hits. He has allowed 8.3 hits per nine innings and his FIP stands at 3.4. So far this season the bullpen has an earned run average of 2.82 and they have given up 43 base hits on the year. Teams are hitting .214 against the Rays bullpen while being struck out 47 times and walking 15 times this season. As a team, Tampa Bay has allowed 7.89 hits per nine innings while striking out 9.55 batters per nine. They are 6th in the league in team earned run average at 3.33. The Rays pitchers as a team have surrendered 147 base knocks and 62 earned runs so far this season. They have given up 21 home runs this year and they give up 1.1 home runs per nine innings as a staff. Tampa Bay as a staff has walked 41 hitters and struck out 178. They give up a walk 2.2 times per 9 innings while they strike out 9.6 per 9. Their team WHIP is 1.12 while their FIP as a staff is 3.41.
As a team, they are batting .224, good for 28th in the league while putting together a .211 average at home. The Rays hold a .391 team slugging percentage and an on-base percentage of .292 which is good for 28th in baseball. They rank 29th in baseball with 7.37 hits per contest. Evan Longoria comes into this matchup batting .253 and he has an OBP of .289. He has 20 hits this year along with 10 runs scored and 9 RBI. He's struck out 16 times and has walked on 4 occasions. Logan Forsythe is hitting .290 and he has an OBP of .364. He has collected 20 hits so far while he's scored 12 runs and drove in 8. He has earned a walk 7 times and has punched out 19 times. The Rays as a unit have 140 base hits, including 32 doubles and 23 homers. They have 8 stolen bases while they've been thrown out 6 times. Tampa Bay as a team has walked 48 times this year and they have struck out 178 times. They've had 121 men left on base and have an OPS of .682. They score 3.53 runs per game and have totaled 67 runs so far this season.
Baltimore Orioles Betting Trends
The Baltimore Orioles are 6-11-1 against the over/under so far this season
The Baltimore Orioles are 10-8-0 against the run line so far this season
Tampa Bay Rays Betting Trends
The Tampa Bay Rays are 5-11-3 against the over/under so far this season
The Tampa Bay Rays are 9-10-0 against the run line so far this season
04/23/16 P Yovani Gallardo Shoulder 15-day DL (4/23)
03/31/16 3B Jimmy Paredes Wrist 15-day DL (3/25)
04/10/16 P Chase Whitley Elbow 60-day DL (3/25)
04/04/16 P Brad Boxberge Abdominal 15-day DL (3/25)
04/01/16 P Alex Cobb Elbow 60-day DL (3/25)
Guy's Pick: Take the Orioles


All of the assignments for MMP 350.
The midterm will combine all of the skills that we have learned so far into one project including Photoshop design, HTML and CSS. Your midterm should be a website with the following files: At least 3 HTML pages (you can use the content from pages of earlier projects). One Photoshop document with a two column, […]	Read post.
The final project for this class is a multimedia website. This will be based on the final project proposal and mockups. Final projects must be uploaded to the FTP server via FileZilla (or another FTP program). The URL should be submitted via Blackboard. Your project should contain: At least 5 HTML pages. 1 CSS page, with […]	Read post.
Color is subjective and dynamic. It can be very meaningful but might signify different meanings or experience for different viewers. Similarly, the way color is displayed physically also changes between mediums. Even with computers, the number of colors, the brightness and the general gamut of color can change from machine to machine. Josef Albers is […]	Read post.
Create a video at least 30 seconds in duration that combines captured video (from a webcam, digital camera or smart phone/PDA) with another source (video, audio, text, images or graphics) edited together in Photoshop.	Read post.
Add sound to your animation. There should be at least 5 sound sources, which can include sound effects, background music, dialog, or any other recordings or samples sound files.	Read post.
Create a keyframe animation in Photoshop using text, graphics, images and motion. The animation should be no shorter than 3o seconds and must contain at least 5 layers with different moving parts. Steps for rendering and submitting your animation Before submitting your animation it needs to be rendered out to a video format. Start by […]	Read post.
Create a splash page for your server with links to your projects. This should be updated throughout the semester with new projects. Extra credit for CSS styles.	Read post.
Add new font styles to your biography website. Use the @import tag to import a font face in your style sheet. Use at least 3 different font treatments. This means three styles that have different sizes, colors, weights or other changes. They can be the same font face.	Read post.
Add an external stylesheet to your biography project, and link it to index.html and two new pages. Upload to the BMCC server and submit the URL to Blackboard.	Read post.
Create a simple HTML page with your biography, including all of the tags from today's lecture and at least one image. Submit this assignment as a zip folder of the index.html file and any image files included in it. Validate your page before turning it in.	Read post.


Choose a chic and versatile piece for the new season with these Verona boots from Carvela Comfort. Featuring a knee high design, these boots are trimmed with elegant wraps at the ankle and set on a stable mid heel. This smooth silhouette is finished with a gentle almond toe.
Crafted to support and cushion your feet all day, wear them with a denim skirt and shirt.