Please use this identifier to cite or link to this item:
|Title:||Crowding alters the folding kinetics of a β-hairpin by modulating the stability of intermediates|
|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|
|Appears in Collections:||Staff Publications|
Show full item record
Files in This Item:
There are no files associated with this item.
checked on Dec 12, 2018
WEB OF SCIENCETM
checked on Dec 4, 2018
checked on Oct 26, 2018
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.