ArticleBiophysical journal2010
Complex unfolding kinetics of single-domain proteins in the presence of force.
Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Slow Transition Path Times Reveal a Complex Folding Barrier in a Designed Protein.Frontiers in chemistry · 2020Article
- Mechanical unfolding of spectrin reveals a super-exponential dependence of unfolding rate on force.Scientific reports · 2019Article
- Connecting thermal and mechanical protein (un)folding landscapes.Biophysical journal · 2014Article
- Direct single-molecule observation of calcium-dependent misfolding in human neuronal calcium sensor-1.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Torsion profiling of proteins using magnetic particles.Biophysical journal · 2013Article
- Using models to design new bioinspired materials.Biophysical journal · 2012Article
- Direct observation of a force-induced switch in the anisotropic mechanical unfolding pathway of a protein.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Direct quantification of the attempt frequency determining the mechanical unfolding of ubiquitin protein.The Journal of biological chemistry · 2011Article
- Mechanically unfolding protein L using a laser-feedback-controlled cantilever.Biophysical journal · 2011Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Single-molecule force spectroscopy is providing unique, and sometimes unexpected, insights into the free-energy landscapes of proteins. Despite the complexity of the free-energy landscapes revealed by mechanical probes, forced unfolding experiments are often analyzed using one-dimensional models that predict a logarithmic dependence of the unfolding force on the pulling velocity. We previously found that the unfolding force of the protein filamin at low pulling speed did not decrease logarithmically with the pulling speed. Here we present results from a large number of unfolding simulations of a coarse-grain model of the protein filamin under a broad range of constant forces. These show that a two-path model is physically plausible and produces a deviation from the behavior predicted by one-dimensional models analogous to that observed experimentally. We also show that the analysis of the distributions of unfolding forces (p[F]) contains crucial and exploitable information, and that a proper description of the unfolding of single-domain proteins needs to account for the intrinsic multidimensionality of the underlying free-energy landscape, especially when the applied perturbation is small.
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