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|Title:||Crowding alters the folding kinetics of a β-hairpin by modulating the stability of intermediates||Authors:||Kurniawan, N.A.
|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|
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