Protein misfolding thermodynamics

Haque, Md Mozzammel ORCID logoORCID: and Bayford, Richard ORCID logoORCID: (2019) Protein misfolding thermodynamics. The Journal of Physical Chemistry Letters, 10 (10) . pp. 2506-2507. ISSN 1948-7185 [Article] (doi:10.1021/acs.jpclett.9b00852)

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It is known that protein misfolding is governed by the hydrophobic effect of solutes at hydrophobic amino acid side chains. The hydrophobic force of nonaqueous solutes acts as a driving force for the spatial rearrangement of protein side chains, whose structural transitions need to be regulated in both time and space. Smaller hydrophobic solutes exert more effect at protein side chains, which involves the clustering of proteins into misfolded shapes. The consequences of misfolding are loss of protein function, gain of toxic function, or both. This is a physical process, whose result has been directly linked to a large number of human diseases.

Item Type: Article
Additional Information: ADDITION / CORRECTION This article has been corrected. View the notice:
Keywords (uncontrolled): General Materials Science
Research Areas: A. > School of Science and Technology > Natural Sciences > Biophysics and Bioengineering group
Item ID: 26662
Notes on copyright: This document is the Accepted Manuscript version of a Published Work that appeared in final form in The Journal of Physical Chemistry Letters, copyright © American Chemical Society after peer review and technical editing by the publisher.
To access the final edited and published work see
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Depositing User: Jisc Publications Router
Date Deposited: 28 May 2019 09:31
Last Modified: 29 Nov 2022 19:07

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