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Title: β-hairpin forms by rolling up from C-terminal: Topological guidance of early folding dynamics
Authors: Enemark, S.
Kurniawan, N.A.
Rajagopalan, R. 
Issue Date: 2012
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
ISSN: 20452322
DOI: 10.1038/srep00649
Appears in Collections:Staff Publications

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