Solvent effects and conformational stability of a tripeptide

被引：0
|
作者：
Fedorov, Maxim V.
Schumm, Stephan
Goodman, Jonathan M.
机构：
[1] Univ Cambridge, Dept Chem, Unilever Ctr Mol Sci Informat, Cambridge CB2 1EW, England
[2] Unilever R&D Vlaardingen, Unilever Food & Hlth Res Inst, NL-3133 AT Vlaardingen, Netherlands
来源：
COMPUTATIONAL LIFE SCIENCES II, PROCEEDINGS | 2006年 / 4216卷
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D O I：
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中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
In this work we are trying to gain an insight on the molecular mechanisms of the salt effects on conformational stability of proteins with use of fully atomistic Molecular Dynamics simulations techniques. Such 'in silico' approach allows us to obtain quite realistic data on the time and scale resolutions that are unavailable for both 'in vitro' and 'in vivo' experimental techniques. We investigated a trialanine peptide which is the one of the simplest examples of biomolecules, bearing the essential features of proteins.
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页码：141 / 149
页数：9
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