ArticleScientific reports2019
Mechanical unfolding of spectrin reveals a super-exponential dependence of unfolding rate on force.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Spectrin coordinates cell shape and signaling essential for epidermal differentiation.The Journal of cell biology · 2026Article
- Mechanical characterization of spectrin at the molecular level.Scientific reports · 2024Article
- Force transmission by retrograde actin flow-induced dynamic molecular stretching of Talin.Nature communications · 2023Article
- De novo design of knotted tandem repeat proteins.Nature communications · 2023Article
- Next Generation Methods for Single-Molecule Force Spectroscopy on Polyproteins and Receptor-Ligand Complexes.Frontiers in molecular biosciences · 2020Review
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Authors and funding
9 authors.
Funding
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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