Urie, Kristopher G. and Angulo, David and Lee, Jennifer C. and Kozak, John J. and Gray, Harry B. and Winkler, Jay R. (2009) Synchronous vs Asynchronous Chain Motion in α-Synuclein Contact Dynamics. Journal of Physical Chemistry B, 113 (2). pp. 522-530. ISSN 1520-6106 http://resolver.caltech.edu/CaltechAUTHORS:URIjpcb09
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α-Synuclein (α-syn) is an intrinsically unstructured 140-residue neuronal protein of uncertain function that is implicated in the etiology of Parkinson’s disease. Tertiary contact formation rate constants in α-syn, determined from diffusion-limited electron-transfer kinetics measurements, are poorly approximated by simple random polymer theory. One source of the discrepancy between theory and experiment may be that interior-loop formation rates are not well approximated by end-to-end contact dynamics models. We have addressed this issue with Monte Carlo simulations to model asynchronous and synchronous motion of contacting sites in a random polymer. These simulations suggest that a dynamical drag effect may slow interior-loop formation rates by about a factor of 2 in comparison to end-to-end loops of comparable size. The additional deviations from random coil behavior in α-syn likely arise from clustering of hydrophobic residues in the disordered polypeptide.
|Additional Information:||Copyright © 2008 American Chemical Society. Received: July 29, 2008; Revised Manuscript Received: October 10, 2008. Publication Date (Web): December 19, 2008. This research was supported by grants from the National Institutes of Health (GM068461 to J.R.W.; DK19038 to H.B.G.) and the Ellison Medical Foundation (Senior Scholar Award in Aging to H.B.G.), and by the Intramural Research Program of the National Institutes of Health, the National Heart, Lung, and Blood Institute (J.C.L.).|
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|Deposited On:||02 Feb 2009 22:18|
|Last Modified:||26 Dec 2012 10:46|
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