期刊
CURRENT PROTEIN & PEPTIDE SCIENCE
卷 9, 期 4, 页码 407-426出版社
BENTHAM SCIENCE PUBL LTD
DOI: 10.2174/138920308785132686
关键词
organic solvents and cosolvents; preferential solvation; protein stability; peptide folding; peptide aggregation; enzymatic catalysis
Pure organic solvents or mixtures with water are very common environments for studying protein and peptide in solution. These milieu conditions are used either for improving the catalytic performance of enzymes or for studying the effect of solvent on the protein stability and hence gaining insight into the protein folding mechanism. The atomic details of these processes are mainly addressed using computer simulation approaches. In particular, Molecular Dynamics simulation represents the most powerful and versatile tool to investigate the details of solvation processes at atomic level. In the last few years, the number of publications peptide and protein simulations in non-natural environments has proliferated. These studies are providing important contributions to shed light on the nature of non-aqueous solvent effects. In this review, the achievements and the future prospects in this field of computational biochemistry are reviewed by summarizing the most important theoretical results published in the last 10 years.
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