Williamson, M.P. and Kitahara, R. (2019) Characterization of low-lying excited states of proteins by high-pressure NMR. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 1867 (3). pp. 350-358. ISSN 1570-9639
Abstract
Hydrostatic pressure alters the free energy of proteins by a few kJ mol-1, with the amount depending on their partial molar volumes. Because the folded ground state of a protein contains cavities, it is always a state of large partial molar volume. Therefore pressure always destabilises the ground state and increases the population of partially and completely unfolded states. This is a mild and reversible conformational change, which allows the study of excited states under thermodynamic equilibrium conditions. Many of the excited states studied in this way are functionally relevant; they also seem to be very similar to kinetic folding intermediates, thus suggesting that evolution has made use of the 'natural' dynamic energy landscape of the protein fold and sculpted it to optimise function. This includes features such as ligand binding, structural change during the catalytic cycle, and dynamic allostery.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2018 Elsevier. This is an author produced version of a paper subsequently published in Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. Uploaded in accordance with the publisher's self-archiving policy. Article available under the terms of the CC-BY-NC-ND licence (https://creativecommons.org/licenses/by-nc-nd/4.0/). |
Keywords: | Allostery; Cavity; Energy landscape; NMR; Pressure; Volume |
Dates: |
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Institution: | The University of Sheffield |
Academic Units: | The University of Sheffield > Faculty of Science (Sheffield) > School of Biosciences (Sheffield) > Department of Molecular Biology and Biotechnology (Sheffield) |
Depositing User: | Symplectic Sheffield |
Date Deposited: | 07 Jan 2019 16:05 |
Last Modified: | 25 Nov 2021 08:50 |
Status: | Published |
Publisher: | Elsevier |
Refereed: | Yes |
Identification Number: | 10.1016/j.bbapap.2018.10.014 |
Related URLs: | |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:140628 |
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Filename: Williamson and Kitahara 2019 preprint.pdf
Licence: CC-BY-NC-ND 4.0