Evidence map›Paper›PMID 19073932›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2008

How main-chains of proteins explore the free-energy landscape in native states.

Patrick Senet, Gia G Maisuradze, Colette Foulie, Patrice Delarue, Harold A Scheraga

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

23 citing papers in PubMed, 55 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Intrinsic Localized Modes in Proteins.Scientific reports · 2015
    Article
  10. My 65 years in protein chemistry.Quarterly reviews of biophysics · 2015
    Review
  11. New Insights into Protein (Un)Folding Dynamics.The journal of physical chemistry letters · 2015
    Article
  12. Accounting for a mirror-image conformation as a subtle effect in protein folding.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  13. Local vs global motions in protein folding.Journal of chemical theory and computation · 2013
    Article
  14. Article
  15. Measurement of energy landscape roughness of folded and unfolded proteins.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  16. Anomalous diffusion and dynamical correlation between the side chains and the main chain of proteins in their native state.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  17. Article
  18. Nonexponential decay of internal rotational correlation functions of native proteins and self-similar structural fluctuations.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  19. Is protein folding sub-diffusive?PLoS computational biology · 2010
    Article
  20. Anomalies in the vibrational dynamics of proteins are a consequence of fractal-like structure.Proceedings of the National Academy of Sciences of the United States of America · 2010
    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 3 institutions in 2 countries.

Patrick SenetBaker Laboratory of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853-1301, USA.
Gia G Maisuradze
Colette Foulie
Patrice Delarue
Harold A Scheraga
Cornell University · USLaboratoire Interdisciplinaire Carnot de Bourgogne · FRUniversité de Bourgogne · FR

Funding

INTERNAL BONDIN IN PROTEINSR01GM014312 · NIGMS · CORNELL UNIVERSITY ITHACA · PI MAISURADZE, GIA, RACKOVSKY, SHALOM R · 1985 to 2021
$9.4M
NIGMS NIH HHS GM-14312NIGMS NIH HHS R01 GM014312
6 · The paper itself

Abstract

Understanding how a single native protein diffuses on its free-energy landscape is essential to understand protein kinetics and function. The dynamics of a protein is complex, with multiple relaxation times reflecting a hierarchical free-energy landscape. Using all-atom molecular dynamics simulations of an alpha/beta protein (crambin) and a beta-sheet polypeptide (BS2) in their "native" states, we demonstrate that the mean-square displacement of dihedral angles, defined by 4 successive C(alpha) atoms, increases as a power law of time, t(alpha), with an exponent alpha between 0.08 and 0.39 (alpha = 1 corresponds to Brownian diffusion), at 300 K. Residues with low exponents are located mainly in well-defined secondary elements and adopt 1 conformational substate. Residues with high exponents are found in loops/turns and chain ends and exist in multiple conformational substates, i.e., they move on multiple-minima free-energy profiles.

Indexed as

EntropyModels, ChemicalProtein FoldingAmino Acid SequencePeptidesPlant ProteinsProtein Structure, Secondarycrambin protein, Crambe abyssinicaPeptidesPlant Proteins

Identifiers

PMID19073932
PMCPMC2604949
OpenAlexW2094509194

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.