ArticleScientific reports2017
Theoretical and computational validation of the Kuhn barrier friction mechanism in unfolded proteins.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed, 35 citations in OpenAlex.
- Static and dynamic rough energy landscapes can lead to identical diffusivity.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Bio-Based Degradable Poly(ether-ester)s from Melt-Polymerization of Aromatic Ester and Ether Diols.International journal of molecular sciences · 2022Article
- Article
- Structural and dynamic characterization of the C-terminal tail of ErbB2: Disordered but not random.Biophysical journal · 2021Article
- Broad distributions of transition-path times are fingerprints of multidimensionality of the underlying free energy landscapes.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Origin of Internal Friction in Disordered Proteins Depends on Solvent Quality.The journal of physical chemistry. B · 2018Article
- Butane dihedral angle dynamics in water is dominated by internal friction.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Single-Molecule Test for Markovianity of the Dynamics along a Reaction Coordinate.The journal of physical chemistry letters · 2018Article
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A long time ago, Kuhn predicted that long polymers should approach a limit where their global motion is controlled by solvent friction alone, with ruggedness of their energy landscapes having no consequences for their dynamics. In contrast, internal friction effects are important for polymers of modest length. Internal friction in proteins, in particular, affects how fast they fold or find their binding targets and, as such, has attracted much recent attention. Here we explore the molecular origins of internal friction in unfolded proteins using atomistic simulations, coarse-grained models and analytic theory. We show that the characteristic internal friction timescale is directly proportional to the timescale of hindered dihedral rotations within the polypeptide chain, with a proportionality coefficient b that is independent of the chain length. Such chain length independence of b provides experimentally testable evidence that internal friction arises from concerted, crankshaft-like dihedral rearrangements. In accord with phenomenological models of internal friction, we find the global reconfiguration timescale of a polypeptide to be the sum of solvent friction and internal friction timescales. At the same time, the time evolution of inter-monomer distances within polypeptides deviates both from the predictions of those models and from a simple, one-dimensional diffusion model.
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