Evidence map›Paper›PMID 20550915›Full record

ArticleBiophysical journal2010

Anharmonic normal mode analysis of elastic network model improves the modeling of atomic fluctuations in protein crystal structures.

Wenjun Zheng

Abstract read
In one paragraph

Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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

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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

12 citing papers in PubMed.

  1. Asymmetric Dynamics Between the Protomers of the σ2 Receptor Homodimer.Journal of chemical information and modeling · 2025
    Article
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  7. Sequence-based Gaussian network model for protein dynamics.Bioinformatics (Oxford, England) · 2014
    Article
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  11. 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

1 author.

Wenjun ZhengPhysics Department, University at Buffalo, Buffalo, New York, USA. wjzheng@buffalo.edu

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein conformational dynamics, despite its significant anharmonicity, has been widely explored by normal mode analysis (NMA) based on atomic or coarse-grained potential functions. To account for the anharmonic aspects of protein dynamics, this study proposes, and has performed, an anharmonic NMA (ANMA) based on the C(alpha)-only elastic network models, which assume elastic interactions between pairs of residues whose C(alpha) atoms or heavy atoms are within a cutoff distance. The key step of ANMA is to sample an anharmonic potential function along the directions of eigenvectors of the lowest normal modes to determine the mean-squared fluctuations along these directions. ANMA was evaluated based on the modeling of anisotropic displacement parameters (ADPs) from a list of 83 high-resolution protein crystal structures. Significant improvement was found in the modeling of ADPs by ANMA compared with standard NMA. Further improvement in the modeling of ADPs is attained if the interactions between a protein and its crystalline environment are taken into account. In addition, this study has determined the optimal cutoff distances for ADP modeling based on elastic network models, and these agree well with the peaks of the statistical distributions of distances between C(alpha) atoms or heavy atoms derived from a large set of protein crystal structures.

Indexed as

ElasticityModels, MolecularAnisotropyCrystallography, X-RayDiphosphotransferasesElectronsEscherichia coliNormal DistributionProtein ConformationProteinsTemperature2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinaseDiphosphotransferasesProteins

Identifiers

PMID20550915
PMCPMC2884254

What OpenQuestion holds

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Read underepoch 390

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.