ArticleBiophysical journal2010
Universality in the timescales of internal loop formation in unfolded proteins and single-stranded oligonucleotides.
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 6 papers.
What it found
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Who cites it
6 citing papers in PubMed.
- Does Electric Friction Matter in Living Cells?The journal of physical chemistry. B · 2021Article
- Theoretical and computational validation of the Kuhn barrier friction mechanism in unfolded proteins.Scientific reports · 2017Article
- Diffusive Dynamics of Contact Formation in Disordered Polypeptides.Physical review letters · 2016Article
- How quickly can a β-hairpin fold from its transition state?The journal of physical chemistry. B · 2014Article
- Sequence and temperature dependence of the end-to-end collision dynamics of single-stranded DNA.Biophysical journal · 2013Article
- Quantifying internal friction in unfolded and intrinsically disordered proteins with single-molecule spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Understanding the rate at which various parts of a molecular chain come together to facilitate the folding of a biopolymer (e.g., a protein or RNA) into its functional form remains an elusive goal. Here we use experiments, simulations, and theory to study the kinetics of internal loop closure in disordered biopolymers such as single-stranded oligonucleotides and unfolded proteins. We present theoretical arguments and computer simulation data to show that the relationship between the timescale of internal loop formation and the positions of the monomers enclosing the loop can be recast in a form of a universal master dependence. We also perform experimental measurements of the loop closure times of single-stranded oligonucleotides and show that both these and previously reported internal loop closure kinetics of unfolded proteins are well described by this theoretically predicted dependence. Finally, we propose that experimental deviations from the master dependence can then be used as a sensitive probe of dynamical and structural order in unfolded proteins and other biopolymers.
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Registered trials
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