The DOI matches its Crossref record; 70 of the 70 references it cites were found in a registry or an index.
Native contacts determine protein folding mechanisms in atomistic simulations
Open accessAbstract
Significance: Understanding the mechanism by which proteins fold to their native structure is a central problem in protein science. Clearly, interactions between residues that are in contact in the folded state (native interactions) are likely to be important for folding, but, in principle, nonnative interactions may play a role. Here, we use recently published microsecond to millisecond all-atom molecular dynamics simulations of proteins folding and unfolding to show, remarkably, that nonnative contacts are irrelevant to the mechanism of folding in most cases. This statistical analysis would be very difficult to perform by experiment. Although this is a limited set of proteins, the results nonetheless strongly support coarse-grained theoretical and simulation models of folding in which only native contacts are energetically favorable.
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Metadata
- Authors
- Best, R. B., Hummer, G., & Eaton, W. A.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2013-10-15
- Volume
- 110
- Issue
- 44
- Pages
- 17874-17879
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2165414288
- Cited by
- 594
- References
- 70
- FWCI
- 15.33
- Type
- journal article
- Language
- en
- Open access
- green
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