A prediction of tertiary structures of peptide by the Monte Carlo simulated annealing method
- 1 November 1989
- journal article
- research article
- Published by Oxford University Press (OUP) in Protein Engineering, Design and Selection
- Vol. 3 (2), 85-94
- https://doi.org/10.1093/protein/3.2.85
Abstract
The Monte Carlo simulated annealing method has been applied to the prediction of three-dimensional structures of enkephalin. The low-energy conformations obtained were classified into a few groups of similar structures, which indicates that our method is effective. New low-energy structures were identified together with previously proposed structures.This publication has 7 references indexed in Scilit:
- Crystallographic refinement by simulated annealingJournal of Molecular Biology, 1988
- Monte Carlo-minimization approach to the multiple-minima problem in protein folding.Proceedings of the National Academy of Sciences, 1987
- An approach to the multiple-minima problem in protein folding by relaxing dimensionalityJournal of Molecular Biology, 1987
- Prediction of the native conformation of a polypeptide by a statistical‐mechanical procedure. III. Probable and average conformations of enkephalinBiopolymers, 1987
- Protein states and proteinquakes.Proceedings of the National Academy of Sciences, 1985
- Crystal structure of leucine-enkephalinNature, 1983
- Enkephalin: conformational analysis by means of empirical energy calculations.Proceedings of the National Academy of Sciences, 1977