Cooperativity, Local-Nonlocal Coupling, and Nonnative Interactions: Principles of Protein Folding from Coarse-Grained Models
Författare
Summary, in English
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.
Publiceringsår
2011
Språk
Engelska
Sidor
301-326
Publikation/Tidskrift/Serie
Annual Review of Physical Chemistry
Volym
62
Länkar
Dokumenttyp
Artikel i tidskrift
Förlag
Annual Reviews
Ämne
- Biophysics
Nyckelord
- native topology
- Levinthal paradox
- folding funnel
- energy landscape
- desolvation
- enthalpic barrier
Status
Published
ISBN/ISSN/Övrigt
- ISSN: 1545-1593