Please use this identifier to cite or link to this item:
https://doi.org/10.1021/ja302943m
Title: | Crowding alters the folding kinetics of a β-hairpin by modulating the stability of intermediates | Authors: | Kurniawan, N.A. Enemark, S. Rajagopalan, R. |
Issue Date: | 20-Jun-2012 | 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 | 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 | Source Title: | Journal of the American Chemical Society | URI: | http://scholarbank.nus.edu.sg/handle/10635/88721 | ISSN: | 00027863 | DOI: | 10.1021/ja302943m |
Appears in Collections: | Staff Publications |
Show full item record
Files in This Item:
There are no files associated with this item.
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.