Stable single α-helices are constant force springs in proteins.

Wolny, M, Batchelor, M, Knight, PJ et al. (3 more authors) (2014) Stable single α-helices are constant force springs in proteins. Journal of Biological Chemistry, 289 (40). 27825 - 27835. ISSN 0021-9258

Abstract

Metadata

Authors/Creators:
  • Wolny, M
  • Batchelor, M
  • Knight, PJ
  • Paci, E
  • Dougan, L
  • Peckham, M
Copyright, Publisher and Additional Information: © 2014 by The American Society for Biochemistry and Molecular Biology, Inc. This is an open access article under the terms of the Creative Commons Attribution License CC BY 3.0
Keywords: Atomic Force Microscopy (AFM); Circular Dichroism (CD); Cytoskeleton; Molecular dynamics; Single α-Helices; Structural biology; Animals; Cattle; Circular dichroism; Microscopy, Atomic force; Models, Molecular; Myosins; Protein folding; Protein structure, Secondary; Protein structure, Tertiary
Dates:
  • Published: 3 October 2014
Institution: The University of Leeds
Academic Units: The University of Leeds > Faculty of Biological Sciences (Leeds)
Depositing User: Symplectic Publications
Date Deposited: 23 Mar 2015 10:44
Last Modified: 23 Mar 2015 10:44
Published Version: http://dx.doi.org/10.1074/jbc.M114.585679
Status: Published
Publisher: American Society for Biochemistry and Molecular Biology
Identification Number: https://doi.org/10.1074/jbc.M114.585679
Related URLs:

Share / Export

Statistics