期刊
CURRENT OPINION IN STRUCTURAL BIOLOGY
卷 18, 期 2, 页码 163-169出版社
CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2007.12.013
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资金
- NEI NIH HHS [PN1 EY016525-02] Funding Source: Medline
- NATIONAL EYE INSTITUTE [PN1EY016525] Funding Source: NIH RePORTER
Chaperonins are known to maintain the stability of the proteome by facilitating the productive folding of numerous misfolded or aggregation-prone proteins and are thus essential for cell viability. Despite their established importance, the mechanism by which chaperonins facilitate protein folding remains unknown. Computer simulation techniques are now being employed to complement experimental ones in order to shed light on this mystery. Here we review previous computational models of chaperonin-mediated protein folding in the context of the two main hypotheses for chaperonin function: iterative annealing and landscape modulation. We then discuss new results pointing to the importance of solvent (a previously neglected factor) in chaperonin activity. We conclude with our views on the future role of simulation in studying chaperonin activity as well as protein folding in other biologically relevant confined contexts.
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