Please use this identifier to cite or link to this item: https://doi.org/10.1039/c2cp40285h
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dc.titleTurn-directed folding dynamics of β-hairpin-forming de novo decapeptide Chignolin
dc.contributor.authorEnemark, S.
dc.contributor.authorRajagopalan, R.
dc.date.accessioned2014-06-17T07:51:00Z
dc.date.available2014-06-17T07:51:00Z
dc.date.issued2012-09-28
dc.identifier.citationEnemark, S., Rajagopalan, R. (2012-09-28). Turn-directed folding dynamics of β-hairpin-forming de novo decapeptide Chignolin. Physical Chemistry Chemical Physics 14 (36) : 12442-12450. ScholarBank@NUS Repository. https://doi.org/10.1039/c2cp40285h
dc.identifier.issn14639076
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/64760
dc.description.abstractRealistic mechanistic pictures of β-hairpin formation, offering valuable insights into some of the key early events in protein folding, are accessible through short designed polypeptides as they allow atomic-level scrutiny through simulations. Here, we present a detailed picture of the dynamics and mechanism of β-hairpin formation of Chignolin, a de novo decapeptide, using extensive, unbiased molecular dynamics simulations. The results provide clear evidence for turn-directed broken-zipper folding and reveal details of turn nucleation and cooperative progression of turn growth, hydrogen-bond formations, and eventual packing of the hydrophobic core. Further, we show that, rather than driving folding through hydrophobic collapse, cross-strand side-chain packing could in fact be rate-limiting as packing frustrations can delay formation of the native hydrophobic core prior to or during folding and even cause relatively long-living misfolded or partially folded states that may nucleate aggregative events in more complex situations. The results support the increasing evidence for turn-centric folding mechanisms for β-hairpin formation suggested recently for GB1 and Peptide 1 based on experiments and simulations but also point to the need for similar examinations of polypeptides with larger numbers of cross-strand hydrophobic residues. This journal is © the Owner Societies 2012.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1039/c2cp40285h
dc.sourceScopus
dc.typeArticle
dc.contributor.departmentCHEMICAL & BIOMOLECULAR ENGINEERING
dc.description.doi10.1039/c2cp40285h
dc.description.sourcetitlePhysical Chemistry Chemical Physics
dc.description.volume14
dc.description.issue36
dc.description.page12442-12450
dc.description.codenPPCPF
dc.identifier.isiut000307900800004
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