Evidence map›Paper›PMID 41589386›Full record

ArticleThe journal of physical chemistry. B2026

The Spatial Distribution of Local Mobility in Folded Proteins.

S Rackovsky

Abstract read
In one paragraph

Article in The journal of physical chemistry. B, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Review
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.

S RackovskyDepartment of Biochemistry and Biophysics, University of Rochester School of Medicine and Dentistry, 601 Elmwood Avenue, Rochester, New York 14642, United States.ORCID 0000-0002-6186-7893

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A quantitative approach is developed to the study of the spatial distribution of amino acid mobility in protein structures. This method, which is based on bioinformatic and signal processing tools, makes it possible to study very large databases of structures simultaneously, and to search for the existence of domains within proteins which are defined by mobility effects, rather than by static structural considerations. It is shown that mobility is distributed nonuniformly in a substantial subset of structures in a large database; that nonuniform mobility distribution does not select for fold class; and that differences in local mobility distribution are correlated with differences in total mobility. Analyzed in light of previous results, these findings suggest that the dynamics of proteins with nonuniform distributions of mobility may exhibit dynamics dominated by local modes, rather than large-scale motions. We suggest that spatial mobility distribution may be a significant driver of protein evolution. It is also speculated that mobility distribution may act as a control on the hydrodynamic environment of proteins in solution.

Indexed as

Protein FoldingProteinsProteins

Identifiers

PMID41589386
PMCPMC12884463

What OpenQuestion holds

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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.