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

J. P. Renn, S. Bhattacharyya, H. Bai, C. He, H. Li, A. F. Oberhauser, J. F. Marko, D. E. Makarov, A. Matouschek

Research output: Contribution to journalArticle

3 Scopus citations

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.

Original languageEnglish (US)
Article number11101
Pages (from-to)11101
Number of pages1
JournalScientific reports
Volume9
Issue number1
DOIs
StatePublished - Jul 31 2019

ASJC Scopus subject areas

  • General

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