A new approach to the rapid determination of protein side chain conformations.

P. Tuffery (1) , C. Etchebest (1) , S. Hazout (1) , R. Lavery (1)

1 IBCP - Institut de biologie et chimie des protéines [Lyon]

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.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.

Domaines: Biochimie, Biologie Moléculaire

P. Tuffery, C. Etchebest, S. Hazout, R. Lavery. A new approach to the rapid determination of protein side chain conformations.. Journal of Biomolecular Structure and Dynamics, 1991, 8, pp.1267-1289. ⟨hal-00313445⟩