A New Approach to the Rapid Determination of Protein Side Chain Conformations
- 1 June 1991
- journal article
- research article
- Published by Taylor & Francis in Journal of Biomolecular Structure and Dynamics
- Vol. 8 (6) , 1267-1289
- https://doi.org/10.1080/07391102.1991.10507882
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.Keywords
This publication has 12 references indexed in Scilit:
- Tertiary templates for proteins: Use of packing criteria in the enumeration of allowed sequences for different structural classesPublished by Elsevier ,2005
- Analysis of the relationship between side-chain conformation and secondary structure in globular proteinsJournal of Molecular Biology, 1987
- Conformational constraints of amino acid side chains in α‐helicesBiopolymers, 1987
- Analysis of side-chain orientations in homologous proteinsJournal of Molecular Biology, 1987
- Prediction of the folding of short polypeptide segments by uniform conformational samplingBiopolymers, 1987
- Optimized monopole expansions for the representation of the electrostatic properties of polypeptides and proteinsJournal of Computational Chemistry, 1985
- Structure and refinement of penicillopepsin at 1.8 Å resolutionJournal of Molecular Biology, 1983
- AN ANALYSIS OF SIDE‐CHAIN CONFORMATION IN PROTEINS*International Journal of Peptide and Protein Research, 1979
- Conformation of amino acid side-chains in proteinsJournal of Molecular Biology, 1978
- The protein data bank: A computer-based archival file for macromolecular structuresJournal of Molecular Biology, 1977