期刊
ANNUAL REVIEW OF PHYSICAL CHEMISTRY, VOL 62
卷 62, 期 -, 页码 301-326出版社
ANNUAL REVIEWS
DOI: 10.1146/annurev-physchem-032210-103405
关键词
native topology; Levinthal paradox; folding funnel; energy landscape; desolvation; enthalpic barrier
资金
- Canadian Institutes of Health Research [MOP-84281] Funding Source: Medline
Coarse-grained, self-contained polymer models are powerful tools in the study of protein folding. They are also essential to assess predictions from less rigorous theoretical approaches that lack an explicit-chain representation. Here we review advances in coarse-grained modeling of cooperative protein folding, noting in particular that the Levinthal paradox was raised in response to the experimental discovery of two-state-like folding in the late 1960s, rather than to the problem of conformational search per se. Comparisons between theory and experiment indicate a prominent role of desolvation barriers in cooperative folding, which likely emerges generally from a coupling between local conformational preferences and nonlocal packing interactions. Many of these principles have been elucidated by native-centric models, wherein nonnative interactions may be treated perturbatively. We discuss these developments as well as recent applications of coarse-grained chain modeling to knotted proteins and to intrinsically disordered proteins.
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