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Pressure-dependent 13C chemical shifts in proteins: Origins and applications

Wilton, D.J., Kitahara, R., Akasaka, A. and Williamson, M.P. (2009) Pressure-dependent 13C chemical shifts in proteins: Origins and applications. Journal of Biomolecular NMR, 44 (1). pp. 25-33. ISSN 0925-2738


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Pressure-dependent (13)C chemical shifts have been measured for aliphatic carbons in barnase and Protein G. Up to 200 MPa (2 kbar), most shift changes are linear, demonstrating pressure-independent compressibilities. CH(3), CH(2) and CH carbon shifts change on average by +0.23, -0.09 and -0.18 ppm, respectively, due to a combination of bond shortening and changes in bond angles, the latter matching one explanation for the gamma-gauche effect. In addition, there is a residue-specific component, arising from both local compression and conformational change. To assess the relative magnitudes of these effects, residue-specific shift changes for protein G were converted into structural restraints and used to calculate the change in structure with pressure, using a genetic algorithm to convert shift changes into dihedral angle restraints. The results demonstrate that residual (13)C alpha shifts are dominated by dihedral angle changes and can be used to calculate structural change, whereas (13)C beta shifts retain significant dependence on local compression, making them less useful as structural restraints.

Item Type: Article
Copyright, Publisher and Additional Information: © 2009 Springer. This is an author produced version of a paper subsequently published in Journal of Biomolecular NMR. Uploaded in accordance with the publisher's self-archiving policy.
Keywords: pressure; 13C chemical shift; genetic algorithm; γ-gauche effect; compression
Institution: The University of Sheffield
Academic Units: The University of Sheffield > Faculty of Science (Sheffield) > School of Biological Sciences (Sheffield) > Department of Molecular Biology and Biotechnology (Sheffield)
Depositing User: Miss Anthea Tucker
Date Deposited: 12 May 2009 13:56
Last Modified: 08 Feb 2013 16:58
Published Version: http://dx.doi.org/10.1007/s10858-009-9312-4
Status: Published
Publisher: Springer Verlag
Refereed: Yes
Identification Number: 10.1007/s10858-009-9312-4
URI: http://eprints.whiterose.ac.uk/id/eprint/8563

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