Please use this identifier to cite or link to this item:
Title: Turn-directed folding dynamics of β-hairpin-forming de novo decapeptide Chignolin
Authors: Enemark, S.
Rajagopalan, R. 
Issue Date: 28-Sep-2012
Citation: Enemark, 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.
Abstract: Realistic 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.
Source Title: Physical Chemistry Chemical Physics
ISSN: 14639076
DOI: 10.1039/c2cp40285h
Appears in Collections:Staff Publications

Show full item record
Files in This Item:
There are no files associated with this item.


checked on Aug 6, 2020


checked on Jul 29, 2020

Page view(s)

checked on Aug 3, 2020

Google ScholarTM



Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.