Thermodynamic stability, unfolding kinetics, and aggregation of the N-terminal actin-binding domains of utrophin and dystrophin.

Singh, S.M., Molas, J.F., Kongari, N. et al. (4 more authors) (2012) Thermodynamic stability, unfolding kinetics, and aggregation of the N-terminal actin-binding domains of utrophin and dystrophin. Proteins, 80 (5). pp. 1377-1392. ISSN 0887-3585

Abstract

Metadata

Authors/Creators:
  • Singh, S.M.
  • Molas, J.F.
  • Kongari, N.
  • Bandi, S.
  • Armstrong, G.S.
  • Winder, S.J.
  • Mallela, K.M.
Copyright, Publisher and Additional Information: © 2012 Wiley. This is an author produced version of a paper subsequently published in Proteins. Uploaded in accordance with the publisher's self-archiving policy.
Keywords: stability; unfolding; aggregation; disease; muscular dystrophy; dystrophin; utrophin; actinbinding domain; calponin-homology domain.
Dates:
  • Published: May 2012
  • Published (online): 17 February 2012
  • Accepted: 2 January 2012
Institution: The University of Sheffield
Academic Units: The University of Sheffield > Faculty of Science (Sheffield) > School of Biological Sciences (Sheffield) > Department of Biomedical Science (Sheffield)
Depositing User: Symplectic Sheffield
Date Deposited: 22 Feb 2017 10:56
Last Modified: 25 Mar 2018 13:21
Published Version: https://doi.org/10.1002/prot.24033
Status: Published
Publisher: Wiley
Refereed: Yes
Identification Number: https://doi.org/10.1002/prot.24033
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