Journal
BIOPHYSICAL JOURNAL
Volume 107, Issue 4, Pages 974-982Publisher
CELL PRESS
DOI: 10.1016/j.bpj.2014.06.046
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Funding
- NIH [R01-GM062868]
- NSF [MCB-0954714]
- Fannie and John Hertz Foundation on the endowed Yaser S. Abu-Mostafa Fellowship
- EPSRC [EP/I003797/1]
- Engineering and Physical Sciences Research Council [EP/I003797/1] Funding Source: researchfish
- EPSRC [EP/I003797/1] Funding Source: UKRI
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Developing an understanding of protein misfolding processes presents a crucial challenge for unlocking the mysteries of human disease. In this article, we present our observations of beta-sheet-rich misfolded states on a number of protein dynamical landscapes investigated through molecular dynamics simulation and Markov state models. We employ a nonequilibrium statistical mechanical theory to identify the glassy states in a protein's dynamics, and we discuss the nonnative, beta-sheet-rich states that play a distinct role in the slowest dynamics within seven protein folding systems. We highlight the fundamental similarity between these states and the amyloid structures responsible for many neurodegenerative diseases, and we discuss potential consequences for mechanisms of protein aggregation and intermolecular amyloid formation.
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