Computer determination of peptide conformations in water: different roads to structure.
收藏PubMed Central1995-04-11 更新2026-05-02 收录
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https://pmc.ncbi.nlm.nih.gov/articles/PMC42131/
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资源简介：
Fragments of proteins (short peptides) that "fold" suggest a mechanism of how complete conformational search in protein folding is avoided. We used a computational method to determine structures of two foldable peptides in explicit water: RVEW and CSVTC. The optimization starts from random structures and no experimental constraints are used. In agreement with NMR data, the simulations find a hydrophobic pair (Val/Trp) in REVW. The structure of CSVTC is induced by a surface water that bridges two amide hydrogens, a drive to structure hypothesized by Ben-Naim [Ben-Naim, A. (1990) J. Chem. Phys. 93, 8196-8210] that is largely ignored in studies of folding. Tendency to structure in short peptide chains suggests a mechanism for the formation of short-range nucleation sites in protein folding. IMAGES:
提供机构：
National Academy of Sciences
创建时间：
1995-04-11
