Lysozyme folded in silico according to the limited conformational sub-space

TitleLysozyme folded in silico according to the limited conformational sub-space
Publication TypeJournal Article
Year of Publication2004
AuthorsJurkowski W, Brylinski M, Konieczny L, Roterman I
JournalJ Biomol Struct Dyn
Volume22
Issue2
Pagination149-58
Date Published2004 Oct
ISSN0739-1102
KeywordsComputer Simulation, Models, Molecular, Muramidase, Protein Conformation, Protein Folding, Software, Thermodynamics
Abstract

The conformational sub-space oriented on early-stage protein folding is applied to lysozyme folding. The part of the Ramachandran map distinguished on the basis of a geometrical model of the polypeptide chain limited to the mutual orientation of the peptide bond planes is shown to deliver the initial structure of the polypeptide for the energy minimization procedure in the ab initio model of protein folding prediction. Two forms of energy minimization and molecular dynamics simulation procedures were applied to the assumed early-stage protein folding of lysozyme. One of them included the disulphide bond system and the other excluded it. The post-energy-minimization and post-dynamics structures were compared using RMS-D and non-bonding contact maps to estimate the degree of approach to the native, target structure of the protein molecule obtained using the limited conformational sub-space for the early stage of folding.

Alternate JournalJournal of Biomolecular Structure & Dynamics
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