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Characterization of folding cores in the cyclophilin A-cyclosporin A complex

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Heal, Jack W., Wells, Stephen A., Blindauer, Claudia A., Freedman, R. B. and Römer, Rudolf A. (2015) Characterization of folding cores in the cyclophilin A-cyclosporin A complex. Biophysical Journal, Volume 108 (Number 7). pp. 1739-1746. doi:10.1016/j.bpj.2015.02.017

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Official URL: http://dx.doi.org/10.1016/j.bpj.2015.02.017

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Abstract

Determining the folding core of a protein yields information about its folding process and dynamics. The experimental procedures for identifying the amino acids that make up the folding core include hydrogen-deuterium exchange and Φ-value analysis and can be expensive and time consuming. Because of this, there is a desire to improve upon existing methods for determining protein folding cores theoretically. We have obtained HDX data for the complex of cyclophilin A with the immunosuppressant cyclosporin A. We compare these data, as well as literature values for uncomplexed cyclophilin A, to theoretical predictions using a combination of rigidity analysis and coarse-grained simulations of protein motion. We find that in this case, the most specific prediction of folding cores comes from a combined approach that models the rigidity of the protein using the first software suite and the dynamics of the protein using the froda tool.

Item Type: Journal Article
Subjects: Q Science > QR Microbiology
Divisions: Other > Institute of Advanced Study
Faculty of Science > Chemistry
Faculty of Science > Life Sciences (2010- )
Faculty of Science > Molecular Organisation and Assembly in Cells (MOAC)
Faculty of Science > Physics
Faculty of Science > Centre for Scientific Computing
Library of Congress Subject Headings (LCSH): Proteins -- Analysis
Journal or Publication Title: Biophysical Journal
Publisher: Biophysical Society
ISSN: 0006-3495
Official Date: 7 April 2015
Dates:
DateEvent
7 April 2015Published
7 April 2015Available
12 February 2015Accepted
27 June 2014Submitted
Volume: Volume 108
Number: Number 7
Number of Pages: 8
Page Range: pp. 1739-1746
DOI: 10.1016/j.bpj.2015.02.017
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Open Access
Funder: International Max Planck Research School (IMPRS), Engineering and Physical Sciences Research Council (EPSRC), University of Warwick. Institute of Advanced Study (IAS)
Grant number: MOAC DTC EP/F500378/1 (EPSRC), EP/K004956/1 (EPSRC)

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