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Sci Rep. 2019 Jul 31;9(1):11101. doi: 10.1038/s41598-019-46525-w.

Mechanical unfolding of spectrin reveals a super-exponential dependence of unfolding rate on force.

Author information

1
Department of Molecular Biosciences, Northwestern University, Evanston, IL 60208, USA.
2
Department of Physics and Astronomy, Northwestern University, Evanston, IL 60208, USA.
3
Department of Chemistry, University of British Columbia, Vancouver, BC, V6T 1Z1, Canada.
4
Department of Neuroscience and Cell Biology, Sealy Center for Structural Biology & Molecular Biophysics, University of Texas Medical Branch, Galveston, TX 77555, USA.
5
Department of Chemistry, The University of Texas at Austin, Austin, TX 78712, USA. makarov@cm.utexas.edu.
6
Oden Institute for Computational Engineering and Sciences, The University of Texas at Austin, Austin, TX 78712, USA. makarov@cm.utexas.edu.
7
Department of Molecular Biosciences, Northwestern University, Evanston, IL 60208, USA. matouschek@austin.utexas.edu.
8
Department of Molecular Biosciences, The University of Texas at Austin, Austin, TX 78712, USA. matouschek@austin.utexas.edu.

Abstract

We investigated the mechanical unfolding of single spectrin molecules over a broad range of loading rates and thus unfolding forces by combining magnetic tweezers with atomic force microscopy. We find that the mean unfolding force increases logarithmically with loading rate at low loading rates, but the increase slows at loading rates above 1pN/s. This behavior indicates an unfolding rate that increases exponentially with the applied force at low forces, as expected on the basis of one-dimensional models of protein unfolding. At higher forces, however, the increase of the unfolding rate with the force becomes faster than exponential, which may indicate anti-Hammond behavior where the structures of the folded and transition states become more different as their free energies become more similar. Such behavior is rarely observed and can be explained by either a change in the unfolding pathway or as a reflection of a multidimensional energy landscape of proteins under force.

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