Please use this identifier to cite or link to this item:
|Title:||β-hairpin forms by rolling up from C-terminal: Topological guidance of early folding dynamics|
|Citation:||Enemark, S., Kurniawan, N.A., Rajagopalan, R. (2012). β-hairpin forms by rolling up from C-terminal: Topological guidance of early folding dynamics. Scientific Reports 2 : -. ScholarBank@NUS Repository.|
|Abstract:||That protein folding is a non-random, guided process has been known even prior to Levinthal's paradox; yet, guided searches, attendant mechanisms and their relation to primary sequence remain obscure. Using extensive molecular dynamics simulations of a β-hairpin with key sequence features similar to those of >13,000 β-hairpins in full proteins, we provide significant insights on the entire pre-folding dynamics at single-residue levels and describe a single, highly coordinated roll-up folding mechanism, with clearly identifiable stages, directing structural progression toward native state. Additional simulations of single-site mutants illustrate the role of three key residues in facilitating this roll-up mechanism. Given the many β-hairpins in full proteins with similar residue arrangements and since β-hairpins are believed to act as nucleation sites in early-stage folding dynamics of full proteins, the topologically guided mechanism seen here may represent one of Nature's strategies for reducing early-stage folding complexity.|
|Source Title:||Scientific Reports|
|Appears in Collections:||Staff Publications|
Show full item record
Files in This Item:
There are no files associated with this item.
checked on Mar 7, 2018
WEB OF SCIENCETM
checked on Apr 16, 2018
checked on Jun 22, 2018
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.