title: A new approach to the rapid determination of protein side chain conformations.
abstract: Two efficient algorithms have been developed which allow amino acid side chain conformations to be optimized rapidly for a given peptide backbone conformation. Both these approaches are based on the assumption that each side chain can be represented by a small number of rotameric states. These states have been obtained by a dynamic cluster analysis of a large data base of known crystallographic structures. Successful applications of these algorithms to the prediction of known protein conformations are presented.
authors.affiliation: Unité de Recherches Biomathématiques et Biostatistiques (INSERM U263) Universitè Paris VII, France.
authors.forename: P
authors.initials: P
authors.lastname: Tuffery
authors.forename: C
authors.initials: C
authors.lastname: Etchebest
authors.forename: S
authors.initials: S
authors.lastname: Hazout
authors.forename: R
authors.initials: R
authors.lastname: Lavery
mesh_terms: D000465:Algorithms; D000595:Amino Acid Sequence; D000596:Amino Acids; D002151:Calorimetry; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000737:chemistry; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*
chemical_list: D000596:Amino Acids; D010940:Plant Proteins; D011506:Proteins; C024934:crambin protein, Crambe abyssinica