Abstract#R##N#Currently, several energy functions and conformational search methods have been developed that are based on the observed distribution of phi and psi angles in protein structures. The definition of phi and psi angles is directly related to the orientation of the peptide plane (CACONHCA). Starting from one conformation and rotating a single peptide plane, the angles psi for one residue and phi for the consecutive residue that are linked by the peptide plane, display a continuous range of values within one global conformation. When peptide plane rotation is analyzed in several different conformations generated from a restricted conformation database, a large number of these conformations are related. Based on these observations, a new simplified all-atom representation for protein folding simulations is presented where only one torsion angle variable is required for each residue. The underlying theme of this article is that conformational search methods using phi and psi torsion space, search through many redundant conformations. These conformations are related by anticorrelated torsion changes of peptide plane rotations. ©1999 John Wiley & Sons, Inc. J Comput Chem 20: 947–955, 1999
['J. M. R. Parker']
The relationship between peptide plane rotation (PPR) and similar conformations