Evidence map›Paper›PMID 27870991›Full record

ReviewCurrent opinion in structural biology2017

Potts Hamiltonian models of protein co-variation, free energy landscapes, and evolutionary fitness.

Ronald M Levy, Allan Haldane, William F Flynn

Abstract readReview
In one paragraph

Review in Current opinion in structural biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing 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

63 citing papers in PubMed.

  1. Article
  2. Beyond native sequence recovery: Improved modeling of the sequence-energy landscape of protein structures.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
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  5. Review
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  15. Article
  16. How the technologies behind self-driving cars, social networks, ChatGPT, and DALL-E2 are changing structural biology.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
    Review
  17. Generating Artificial Ribozymes Using Sparse Coevolutionary Models.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  18. Article
  19. Article
  20. Review

3 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

3 authors.

Ronald M LevyCenter for Biophysics and Computational Biology, Department of Chemistry, and Institute for Computational Molecular Science, Temple University, Philadelphia, PA 19122, United States. Electronic address: ronlevy@temple.edu.
Allan HaldaneCenter for Biophysics and Computational Biology, Department of Chemistry, and Institute for Computational Molecular Science, Temple University, Philadelphia, PA 19122, United States.
William F FlynnCenter for Biophysics and Computational Biology, Department of Chemistry, and Institute for Computational Molecular Science, Temple University, Philadelphia, PA 19122, United States; Department of Physics and Astronomy, Rutgers, The State University of New Jersey, Piscataway, NJ 08854, United States.

Funding

Project 9P50GM103368 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI ARNOLD, EDWARD · 2012 to 2016
$20.0M
DYNAMICS OF PEPTIDES AND PROTEINSR01GM030580 · NIGMS · TEMPLE UNIV OF THE COMMONWEALTH · PI LEVY, RONALD · 1985 to 2018
$6.1M
NIGMS NIH HHS P50 GM103368NIGMS NIH HHS R01 GM030580
6 · The paper itself

Abstract

Potts Hamiltonian models of protein sequence co-variation are statistical models constructed from the pair correlations observed in a multiple sequence alignment (MSA) of a protein family. These models are powerful because they capture higher order correlations induced by mutations evolving under constraints and help quantify the connections between protein sequence, structure, and function maintained through evolution. We review recent work with Potts models to predict protein structure and sequence-dependent conformational free energy landscapes, to survey protein fitness landscapes and to explore the effects of epistasis on fitness. We also comment on the numerical methods used to infer these models for each application.

Indexed as

Evolution, MolecularModels, MolecularEpistasis, GeneticProteinsThermodynamicsProteins

Identifiers

PMID27870991
PMCPMC5869684

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.