ArticlePhysical review letters2014
Evidence of disorder in biological molecules from single molecule pulling experiments.
Article in Physical review letters, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Identical sequences, different behaviors: Protein diversity captured at the single-molecule level.Biophysical journal · 2024Article
- Mechanical Unfolding of Single Polyubiquitin Molecules Reveals Evidence of Dynamic Disorder.ACS omega · 2020Article
- Dynamic coordination of two-metal-ions orchestrates λ-exonuclease catalysis.Nature communications · 2018Article
- Regulatory element in fibrin triggers tension-activated transition from catch to slip bonds.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Heterogeneity in kinesin function.Traffic (Copenhagen, Denmark) · 2017Article
- Conformational dynamics of the frameshift stimulatory structure in HIV-1.RNA (New York, N.Y.) · 2017Article
- Decoding Single Molecule Time Traces with Dynamic Disorder.PLoS computational biology · 2016Article
- Directly measuring single-molecule heterogeneity using force spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Contact Statistics Highlight Distinct Organizing Principles of Proteins and RNA.Biophysical journal · 2016Article
- Molecular investigations into the mechanics of a muscle anchoring complex.Biophysical journal · 2015Article
- Cation-induced kinetic heterogeneity of the intron-exon recognition in single group II introns.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Heterogeneity in biological molecules, resulting in molecule-to-molecule variations in their dynamics and function, is an emerging theme. To elucidate the consequences of heterogeneous behavior at the single molecule level, we propose an exactly solvable model in which the unfolding rate due to mechanical force depends parametrically on an auxiliary variable representing an entropy barrier arising from fluctuations in internal dynamics. When the rate of fluctuations--a measure of dynamical disorder--is comparable to or smaller than the rate of force-induced unbinding, we show that there are two experimentally observable consequences: nonexponential survival probability at constant force, and a heavy-tailed rupture force distribution at constant loading rate. By fitting our analytical expressions to data from single molecule pulling experiments on proteins and DNA, we quantify the extent of disorder. We show that only by analyzing data over a wide range of forces and loading rates can the role of disorder due to internal dynamics be quantitatively assessed.
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