Analysis of Conformations of Amino Acid Residues and Prediction of Backbone Topography in Proteins

Abstract

Methods for describing a discrete number of conformational states of amino acid residues in proteins are presented and used to investigate the topography of chain folding. The relative importance of short‐range, medium‐range and long‐range interactions is discussed in the light of an analysis of the conformational states for the different amino acid residues in eight proteins of known structure. A prediction algorithm, which assigns four states to each residue of a protein chain (α‐helix, extended structure, bend, or coil), has been developed from a consideration of both short‐ and medium‐range interactions and applied to thirteen proteins of known three‐dimensional structure. The prediction..