Evidence map›Paper›PMID 32937108›Full record

ArticleBiophysical journal2020

Sequence-Based Prediction of Metamorphic Behavior in Proteins.

Nanhao Chen, Madhurima Das, Andy LiWang, Lee-Ping Wang

Abstract read
In one paragraph

Article in Biophysical journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

  1. Fold-Switching Proteins.Annual review of biophysics · 2026
    Review
  2. Article
  3. Article
  4. Article
  5. Unveiling the cold reality of metamorphic proteins.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  6. Article
  7. Article
  8. Temperature-dependent fold-switching mechanism of the circadian clock protein KaiB.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  9. Article
  10. Fluid protein fold space and its implications.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023
    Article
  11. Distinguishing features of fold-switching proteins.Protein science : a publication of the Protein Society · 2023
    Review
  12. Article
  13. Article
  14. AlphaFold2 fails to predict protein fold switching.Protein science : a publication of the Protein Society · 2022
    Article
  15. Review
  16. Article
  17. Article
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.

Nanhao ChenDepartment of Chemistry, University of California, Davis, California.
Madhurima DasSchool of Natural Sciences, University of California, Merced, California.
Andy LiWangSchool of Natural Sciences, University of California, Merced, California; Chemistry & Chemical Biology, University of California, Merced, California; Center for Cellular and Biomolecular Machines, University of California, Merced, California; Center for Circadian Biology, University of California, San Diego, La Jolla, California; Quantitative & Systems Biology, University of California, Merced, California; Health Sciences Research Institute, University of California, Merced, California.
Lee-Ping WangDepartment of Chemistry, University of California, Davis, California. Electronic address: leeping@ucdavis.edu.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

An increasing number of proteins have been demonstrated in recent years to adopt multiple three-dimensional folds with different functions. These metamorphic proteins are characterized by having two or more folds with significant differences in their secondary structure, in which each fold is stabilized by a distinct local environment. So far, ∼90 metamorphic proteins have been identified in the Protein Databank, but we and others hypothesize that a far greater number of metamorphic proteins remain undiscovered. In this work, we introduce a computational model to predict metamorphic behavior in proteins using only knowledge of the sequence. In this model, secondary structure prediction programs are used to calculate diversity indices, which are measures of uncertainty in predicted secondary structure at each position in the sequence; these are then used to assign protein sequences as likely to be metamorphic versus monomorphic (i.e., having just one fold). We constructed a reference data set to train our classification method, which includes a novel compilation of 136 likely monomorphic proteins and a set of 201 metamorphic protein structures taken from the literature. Our model is able to classify proteins as metamorphic versus monomorphic with a Matthews correlation coefficient of ∼0.36 and true positive/true negative rates of ∼65%/80%, suggesting that it is possible to predict metamorphic behavior in proteins using only sequence information.

Indexed as

Protein FoldingProteinsAmino Acid SequenceDatabases, ProteinProtein Structure, SecondaryProteins

Identifiers

PMID32937108
PMCPMC7567988

What OpenQuestion holds

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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.