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|Title:||Turn-directed folding dynamics of β-hairpin-forming de novo decapeptide Chignolin||Authors:||Enemark, S.
|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||URI:||http://scholarbank.nus.edu.sg/handle/10635/90437||ISSN:||14639076|
|Appears in Collections:||Staff Publications|
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