Signatures of protein fold switching in the unfolded state.

David Wang, Robert B Best

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In one paragraph

Article in Biophysical journal, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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5 · Who and what money

Authors and funding

2 authors.

David WangLaboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA; Department of Biology, Johns Hopkins University, Baltimore, MD 21218, USA.

Robert B BestLaboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA. Electronic address: robert.best2@nih.gov.

Funding

Understanding protein folding, evolution and function via molecular simulationZIADK075104 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI BEST, ROBERT · 2013 to 2025

$13.7M

Resource for Biocomputing Visualization and InformaticsP41GM103311 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FERRIN, THOMAS E · 2012 to 2017

$8.2M

Intramural NIH HHS Z99 DK999999Intramural NIH HHS ZIA DK075104NIGMS NIH HHS P41 GM103311

6 · The paper itself

Abstract

We have recently shown that, in simulations of unfolded globular proteins, the native contacts are distinguished by their mutual cooperativity, such that this can be used to identify native contact networks. Here, we use this approach to analyze the unfolded states of fold-switching proteins. For a series of designed fold-switching proteins bridging the GA and GB folds, we observe a systematic shift in the networks of cooperative contacts between those of the α and α/β folds. For the naturally occurring fold-switcher RfaH, we also observe that the cooperativities of the contacts corresponding to the alternative folds are much more similar in energy than in the case of the related NusG, which does not switch folds. The results suggest that the signatures of cooperativity of alternative folds encoded by fold-switching sequences are already present in the unfolded state.

Indexed as

Protein FoldingProteinsProtein UnfoldingModels, MolecularThermodynamicsProteins

Identifiers

PMID42310953

DOI10.1016/j.bpj.2026.06.018

PMCPMC13318271

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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.