Evidence map›Paper›PMID 17158578›Full record

ArticleBiophysical journal2007

Entropy and barrier-controlled fluctuations determine conformational viscoelasticity of single biomolecules.

Bhavin S Khatri, Masaru Kawakami, Katherine Byrne, D Alastair Smith, Tom C B McLeish

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
3.9field-weighted citation impact, top 7% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

11 citing papers in PubMed, 55 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Conformational entropy of a single peptide controlled under force governs protease recognition and catalysis.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  5. Unwinding and rewinding the nucleosome inner turn: force dependence of the kinetic rate constants.Physical review. E, Statistical, nonlinear, and soft matter physics · 2013
    Article
  6. Review
  7. Article
  8. Deconvolution of dynamic mechanical networks.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  9. Article
  10. Article
  11. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Bhavin S KhatriInstitute of Molecular Biophysics & Polymer and Complex Fluids Group, School of Physics and Astronomy, University of Leeds, Leeds, United Kingdom.
Masaru Kawakami
Katherine Byrne
D Alastair Smith
Tom C B McLeish
University of Leeds · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Biological macromolecules have complex and nontrivial energy landscapes, endowing them with a unique conformational adaptability and diversity in function. Hence, understanding the processes of elasticity and dissipation at the nanoscale is important to molecular biology and emerging fields such as nanotechnology. Here we analyze single molecule fluctuations in an atomic force microscope, using a generic model of biopolymer viscoelasticity that includes local "internal" conformational dissipation. Comparing two biopolymers, dextran and cellulose (polysaccharides with and without local bistable transitions), demonstrates that signatures of simple conformational change are minima in both the elastic and internal friction constants around a characteristic force. A novel analysis of dynamics on a bistable energy landscape provides a simple explanation: an elasticity driven by the entropy, and friction by a barrier-controlled hopping time of populations between states, which is surprisingly distinct to the well-known relaxation time. This nonequilibrium microscopic analysis thus provides a means of quantifying new dynamical features of the energy landscape of the glucopyranose ring, revealing an unexpected underlying roughness and information on the shape of the barrier of the chair-boat transition in dextran. The results presented herein provide a basis toward probing the viscoelasticity of macromolecular conformational transitions on more complex energy landscapes, such as during protein folding.

Indexed as

Models, ChemicalModels, MolecularBiopolymersComputer SimulationElasticityEnergy TransferEntropyMicromanipulationMicroscopy, Atomic ForceMolecular ConformationStress, MechanicalViscosityBiopolymers

Identifiers

PMID17158578
PMCPMC1861772
OpenAlexW1998308820

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.