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
Single α-helix (SAH) domains are rich in charged residues (Arg, Lys, and Glu) and stable in solution over a wide range of pH and salt concentrations. They are found in many different proteins where they bridge two functional domains. To test the idea that their high stability might enable these proteins to resist unfolding along their length, the properties and unfolding behavior of the predicted SAH domain from myosin-10 were characterized. The expressed and purified SAH domain was highly helical, melted non-cooperatively, and was monomeric as shown by circular dichroism and mass spectrometry as expected for a SAH domain. Single molecule force spectroscopy experiments showed that the SAH domain unfolded at very low forces (<30 pN) without a characteristic unfolding peak. Molecular dynamics simulations showed that the SAH domain unfolds progressively as the length is increased and refolds progressively as the length is reduced. This enables the SAH domain to act as a constant force spring in the mechanically dynamic environment of the cell.
Metadata
Item Type: | Article |
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Authors/Creators: |
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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: |
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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: | 10.1074/jbc.M114.585679 |
Related URLs: | |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:83658 |