A new approach to the rapid determination of protein side chain conformations.
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.
Tuffery
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P
Unité de Recherches Biomathématiques et Biostatistiques (INSERM U263) Universitè Paris VII, France.
Etchebest
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C
Hazout
S
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Lavery
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R
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*
D000596:Amino Acids; D010940:Plant Proteins; D011506:Proteins; C024934:crambin protein, Crambe abyssinica