Protein misfolding thermodynamics
Article
Haque, M. and Bayford, R. 2019. Protein misfolding thermodynamics. The Journal of Physical Chemistry Letters. 10 (10), pp. 2506-2507. https://doi.org/10.1021/acs.jpclett.9b00852
Type | Article |
---|---|
Title | Protein misfolding thermodynamics |
Authors | Haque, M. and Bayford, R. |
Abstract | 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. |
Keywords | General Materials Science |
Research Group | Biophysics and Bioengineering group |
Publisher | American Chemical Society (ACS) |
Journal | The Journal of Physical Chemistry Letters |
ISSN | 1948-7185 |
Publication dates | |
Online | 16 May 2019 |
16 May 2019 | |
Publication process dates | |
Deposited | 28 May 2019 |
Accepted | 30 Apr 2019 |
Output status | Published |
Accepted author manuscript | |
Copyright Statement | 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. |
Additional information | ADDITION / CORRECTION This article has been corrected. View the notice: https://pubs.acs.org/doi/10.1021/acs.jpclett.9b01444 |
Digital Object Identifier (DOI) | https://doi.org/10.1021/acs.jpclett.9b00852 |
Language | English |
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