Please use this identifier to cite or link to this item:
https://doi.org/10.1021/ja302943m
DC Field | Value | |
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dc.title | Crowding alters the folding kinetics of a β-hairpin by modulating the stability of intermediates | |
dc.contributor.author | Kurniawan, N.A. | |
dc.contributor.author | Enemark, S. | |
dc.contributor.author | Rajagopalan, R. | |
dc.date.accessioned | 2014-10-09T06:45:34Z | |
dc.date.available | 2014-10-09T06:45:34Z | |
dc.date.issued | 2012-06-20 | |
dc.identifier.citation | Kurniawan, N.A., Enemark, S., Rajagopalan, R. (2012-06-20). Crowding alters the folding kinetics of a β-hairpin by modulating the stability of intermediates. Journal of the American Chemical Society 134 (24) : 10200-10208. ScholarBank@NUS Repository. https://doi.org/10.1021/ja302943m | |
dc.identifier.issn | 00027863 | |
dc.identifier.uri | http://scholarbank.nus.edu.sg/handle/10635/88721 | |
dc.description.abstract | Crowded environments inside cells exert significant effects on protein structure, stability, and function, but their effects on (pre)folding dynamics and kinetics, especially at molecular levels, remain ill-understood. Here, we examine the latter for, as an initial candidate, a small de novo β-hairpin using extensive all-atom molecular dynamics simulations for crowder volume fractions φ up to 40%. We find that crowding does not introduce new folding intermediates or misfolded structures, although, as expected, it promotes compact structures and reduces the accessible conformational space. Furthermore, while hydrophobic-collapse-mediated folding is slightly enhanced, the turn-directed zipper mechanism (dominant in crowder-free situations) increases many-fold, becoming even more dominant. Interestingly, φ influences the stability of the folding intermediates (FI 1 and FI 2) in an apparently counterintuitive manner, which can be understood only by considering specific intrachain interactions and intermediate (and hierarchical) structural transitions. For φ values | |
dc.description.uri | http://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1021/ja302943m | |
dc.source | Scopus | |
dc.type | Article | |
dc.contributor.department | CHEMICAL & BIOMOLECULAR ENGINEERING | |
dc.description.doi | 10.1021/ja302943m | |
dc.description.sourcetitle | Journal of the American Chemical Society | |
dc.description.volume | 134 | |
dc.description.issue | 24 | |
dc.description.page | 10200-10208 | |
dc.description.coden | JACSA | |
dc.identifier.isiut | 000305358900060 | |
Appears in Collections: | Staff Publications |
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