Evidence map›Paper›PMID 15987905›Full record

ArticleProtein science : a publication of the Protein Society2005

Protein flexibility prediction by an all-atom mean-field statistical theory.

B P Pandey, Chi Zhang, Xianzhang Yuan, Jian Zi, Yaoqi Zhou

Abstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing 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

9 citing papers in PubMed.

  1. In-silico inquest reveal the efficacy ofIn silico pharmacology · 2025
    Article
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  4. Review
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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.

B P PandeyHoward Hughes Medical Institute Center for Single Molecule Biophysics and Department of Physiology and Biophysics, State University of New York at Buffalo, 14214, USA.
Chi Zhang
Xianzhang Yuan
Jian Zi
Yaoqi Zhou

Funding

Development &Applications of Knowledge-based PotentialsR01GM068530 · NIGMS · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI ZHOU, YAOQI · 2003 to 2006
$928k
NIGMS NIH HHS R01 GM 068530NIGMS NIH HHS R01 GM068530NIGMS NIH HHS R01 GM 966049
6 · The paper itself

Abstract

We extended a mean-field model to proteins with all atomic detail. The all-atom mean-field model was used to calculate the dynamic and thermodynamic properties of a three-helix bundle fragment of Staphylococcal protein A (Protein Data Bank [PDB] ID 1BDD) and alpha-spectrin SH3 domain protein (PDB ID 1SHG). We show that a model with all-atomic detail provides a significantly more accurate prediction of flexibility of residues in proteins than does a coarse-grained residue-level model. The accuracy of flexibility prediction is further confirmed by application of the method to 18 additional proteins with the largest size of 224 residues.

Indexed as

Models, StatisticalModels, TheoreticalMathematicsModels, ChemicalModels, MolecularProtein BindingProtein FoldingProtein Structure, SecondarySpectrinsrc Homology DomainsStaphylococcal Protein AThermodynamicsSpectrinStaphylococcal Protein A

Identifiers

PMID15987905
PMCPMC2253361

What OpenQuestion holds

Textmetadata
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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.