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|Title:||Precursory signatures of protein folding/unfolding : from time series correlation analysis to atomistic mechanisms||Authors:||Hsu, P. J.
Cheong, S. A.
Lai, S. K.
|Keywords:||DRNTU::Science||Issue Date:||2014||Source:||Hsu, P. J., Cheong, S. A., & Lai, S. K. (2014). Precursory signatures of protein folding/unfolding: From time series correlation analysis to atomistic mechanisms. The Journal of Chemical Physics, 140(20), 204905-.||Series/Report no.:||The journal of chemical physics||Abstract:||Folded conformations of proteins in thermodynamically stable states have long lifetimes. Before it folds into a stable conformation, or after unfolding from a stable conformation, the protein will generally stray from one random conformation to another leading thus to rapid fluctuations. Brief structural changes therefore occur before folding and unfolding events. These short-lived movements are easily overlooked in studies of folding/unfolding for they represent momentary excursions of the protein to explore conformations in the neighborhood of the stable conformation. The present study looks for precursory signatures of protein folding/unfolding within these rapid fluctuations through a combination of three techniques: (1) ultrafast shape recognition, (2) time series segmentation, and (3) time series correlation analysis. The first procedure measures the differences between statistical distance distributions of atoms in different conformations by calculating shape similarity indices from molecular dynamics simulation trajectories. The second procedure is used to discover the times at which the protein makes transitions from one conformation to another. Finally, we employ the third technique to exploit spatial fingerprints of the stable conformations; this procedure is to map out the sequences of changes preceding the actual folding and unfolding events, since strongly correlated atoms in different conformations are different due to bond and steric constraints. The aforementioned high-frequency fluctuations are therefore characterized by distinct correlational and structural changes that are associated with rate-limiting precursors that translate into brief segments. Guided by these technical procedures, we choose a model system, a fragment of the protein transthyretin, for identifying in this system not only the precursory signatures of transitions associated with α helix and β hairpin, but also the important role played by weaker correlations in such protein folding dynamics.||URI:||https://hdl.handle.net/10356/103714
|ISSN:||0021-9606||DOI:||http://dx.doi.org/10.1063/1.4875802||Rights:||© 2014 AIP Publishing LLC. This paper was published in The Journal of Chemical Physics and is made available as an electronic reprint (preprint) with permission of AIP Publishing LLC. The paper can be found at the following official DOI: http://dx.doi.org/10.1063/1.4875802. One print or electronic copy may be made for personal use only. Systematic or multiple reproduction, distribution to multiple locations via electronic or other means, duplication of any material in this paper for a fee or for commercial purposes, or modification of the content of the paper is prohibited and is subject to penalties under law.||Fulltext Permission:||open||Fulltext Availability:||With Fulltext|
|Appears in Collections:||SPMS Journal Articles|
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