Evidence map›Paper›PMID 22427707›Full record

ArticleMolecular biology and evolution2012

Sequence evolution correlates with structural dynamics.

Ying Liu, Ivet Bahar

Abstract read
In one paragraph

Article in Molecular biology and evolution, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.

0numbers the graph read from it
0cells of the map it votes in
76citing 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

76 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Accurate identification and mechanistic evaluation of pathogenic missense variants withProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  6. Article
  7. Biotechnologia · 2025
    Article
  8. Reused Protein Segments Linked to Functional Dynamics.Molecular biology and evolution · 2024
    Article
  9. Article
  10. Review
  11. Genome-Wide Identification ofInternational journal of molecular sciences · 2023
    Article
  12. Article
  13. Article
  14. Functional Protein Dynamics Directly from Sequences.The journal of physical chemistry. B · 2023
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

16 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.

Ying LiuDepartment of Computational and Systems Biology, School of Medicine, University of Pittsburgh, PA, USA.
Ivet Bahar

Funding

Bridging Sequence Patterns and Structural DynamicsR01LM007994 · NLM · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI BAHAR, IVET · 2004 to 2011
$3.0M
NLM NIH HHS 5R01LM007994-07NLM NIH HHS R01 LM007994
6 · The paper itself

Abstract

Biochemical activity and core stability are essential properties of proteins, maintained usually by conserved amino acids. Structural dynamics emerged in recent years as another essential aspect of protein functionality. Structural dynamics enable the adaptation of the protein to binding substrates and to undergo allosteric transitions, while maintaining the native fold. Key residues that mediate structural dynamics would thus be expected to be conserved or exhibit coevolutionary patterns at least. Yet, the correlation between sequence evolution and structural dynamics is yet to be established. With recent advances in efficient characterization of structural dynamics, we are now in a position to perform a systematic analysis. In the present study, a set of 34 enzymes representing various folds and functional classes is analyzed using information theory and elastic network models. Our analysis shows that the structural regions distinguished by their coevolution propensity as well as high mobility are predisposed to serve as substrate recognition sites, whereas residues acting as global hinges during collective dynamics are often supported by conserved residues. We propose a mobility scale for different types of amino acids, which tends to vary inversely with amino acid conservation. Our findings suggest the balance between physical adaptability (enabled by structure-encoded motions) and chemical specificity (conferred by correlated amino acid substitutions) underlies the selection of a relatively small set of versatile folds by proteins.

Indexed as

Evolution, MolecularProtein ConformationAmino AcidsAmino Acid SequenceCluster AnalysisConserved SequenceEnzymesLigandsModels, MolecularProtein BindingProteinsSubstrate SpecificityAmino AcidsEnzymesLigandsProteins

Identifiers

PMID22427707
PMCPMC3424413

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.