Evidence map›Paper›PMID 19399227›Full record

ReviewInternational journal of molecular sciences2009

Insights from coarse-grained Gō models for protein folding and dynamics.

Ronald D Hills, Charles L Brooks

Abstract readReview
In one paragraph

Review in International journal of molecular sciences, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 87 papers.

0numbers the graph read from it
0cells of the map it votes in
87citing papers in PubMed
–field-weighted citation impact
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

87 citing papers in PubMed.

  1. Article
  2. Article
  3. Simulating biomolecules for physiological timescales.Current opinion in structural biology · 2025
    Review
  4. Article
  5. Machine learning meets physics: A two-way street.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  6. Folding kinetics of an entangled protein.PLoS computational biology · 2023
    Article
  7. Entangled Motifs in Membrane Protein Structures.International journal of molecular sciences · 2023
    Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Review
  19. Review
  20. Article

27 more citing papers are in PubMed but not listed here.

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

2 authors.

Ronald D HillsDepartment of Molecular Biology and Kellogg School of Science and Technology, The Scripps Research Institute, 10550 N. Torrey Pines Rd. TPC6 La Jolla, CA 92037, USA.
Charles L BrooksDepartment of Molecular Biology and Kellogg School of Science and Technology, The Scripps Research Institute, 10550 N. Torrey Pines Rd. TPC6 La Jolla, CA 92037, USA.

Funding

PROTEIN FOLDING THERMODYNAMICS AND KINETICSR01GM048807 · NIGMS · SCRIPPS RESEARCH INSTITUTE · PI BROOKS, CHARLES L · 1994 to 2005
$1.9M
New Technologies for Patch-Clamp RecordingR01EB002020 · NIBIB · YALE UNIVERSITY · PI SIGWORTH, FREDERICK J · 2003 to 2005
$833k
NIBIB NIH HHS R01 EB002020NIGMS NIH HHS R01 GM048807
6 · The paper itself

Abstract

Exploring the landscape of large scale conformational changes such as protein folding at atomistic detail poses a considerable computational challenge. Coarse-grained representations of the peptide chain have therefore been developed and over the last decade have proved extremely valuable. These include topology-based Gō models, which constitute a smooth and funnel-like approximation to the folding landscape. We review the many variations of the Gō model that have been employed to yield insight into folding mechanisms. Their success has been interpreted as a consequence of the dominant role of the native topology in folding. The role of local contact density in determining protein dynamics is also discussed and is used to explain the ability of Gō-like models to capture sequence effects in folding and elucidate conformational transitions.

Indexed as

Models, MolecularKineticsProtein FoldingProteinsProteinscoarse-grainingconformational transitionsenergy landscapeGō modelsProtein folding

Identifiers

PMID19399227
PMCPMC2672008

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Registered trials

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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.