Int. J. Mol. Sci. 2016, 17(11), 1896; doi:10.3390/ijms17111896
Effect of Post-Translational Amidation on Islet Amyloid Polypeptide Conformational Ensemble: Implications for Its Aggregation Early Steps
BioCIS, Université Paris-Sud, CNRS, Université Paris-Saclay, 92290 Châtenay-Malabry, France
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Academic Editor: Cheorl-Ho Kim
Received: 22 September 2016 / Revised: 2 November 2016 / Accepted: 9 November 2016 / Published: 14 November 2016
(This article belongs to the Section Biochemistry, Molecular and Cellular Biology)
Abstract
The human islet amyloid polypeptide (hIAPP) is an intrinsically disordered protein that can self-assemble into fibrillar aggregates that play a key role in the pathogenesis of the type II diabetes mellitus. hIAPP can transiently adoptKeywords:
IAPP; intrinsically disordered protein; transient secondary structures; replica exchange molecular dynamics; conformational selection mechanism
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Tran, L.; Ha-Duong, T. Effect of Post-Translational Amidation on Islet Amyloid Polypeptide Conformational Ensemble: Implications for Its Aggregation Early Steps. Int. J. Mol. Sci. 2016, 17, 1896.
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