Evidence map›Paper›PMID 28402878›Full record

ArticleBiophysical journal2017

The Role of Evolutionary Selection in the Dynamics of Protein Structure Evolution.

Amy I Gilson, Ahmee Marshall-Christensen, Jeong-Mo Choi, Eugene I Shakhnovich

Abstract read
In one paragraph

Article in Biophysical journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing 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

26 citing papers in PubMed.

  1. Allelic diversity ofVeterinary and animal science · 2025
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  16. Exposing the distinctive modular behavior of β-strands and α-helices in folded proteins.Proceedings of the National Academy of Sciences of the United States of America · 2020
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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

4 authors.

Amy I GilsonDepartment of Chemistry and Chemical Biology, Harvard University, Cambridge, Massachusetts.
Ahmee Marshall-ChristensenDepartment of Chemistry and Chemical Biology, Harvard University, Cambridge, Massachusetts.
Jeong-Mo ChoiDepartment of Chemistry and Chemical Biology, Harvard University, Cambridge, Massachusetts.
Eugene I ShakhnovichDepartment of Chemistry and Chemical Biology, Harvard University, Cambridge, Massachusetts. Electronic address: shakhnovich@chemistry.harvard.edu.

Funding

Study of Biological Evolution of Structure and Function in ProteinsR01GM068670 · NIGMS · HARVARD UNIVERSITY · PI SHAKHNOVICH, EUGENE I · 2004 to 2020
$7.0M
NIGMS NIH HHS R01 GM068670
6 · The paper itself

Abstract

Homology modeling is a powerful tool for predicting a protein's structure. This approach is successful because proteins whose sequences are only 30% identical still adopt the same structure, while structure similarity rapidly deteriorates beyond the 30% threshold. By studying the divergence of protein structure as sequence evolves in real proteins and in evolutionary simulations, we show that this nonlinear sequence-structure relationship emerges as a result of selection for protein folding stability in divergent evolution. Fitness constraints prevent the emergence of unstable protein evolutionary intermediates, thereby enforcing evolutionary paths that preserve protein structure despite broad sequence divergence. However, on longer timescales, evolution is punctuated by rare events where the fitness barriers obstructing structure evolution are overcome and discovery of new structures occurs. We outline biophysical and evolutionary rationale for broad variation in protein family sizes, prevalence of compact structures among ancient proteins, and more rapid structure evolution of proteins with lower packing density.

Indexed as

Evolution, MolecularSelection, GeneticComputer SimulationModels, MolecularMonte Carlo MethodProtein DomainsProteinsProtein StabilityProtein Structure, SecondaryStructure-Activity RelationshipProteins

Identifiers

PMID28402878
PMCPMC5390048

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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.