Dynamics-based protein network features accurately discriminate neutral and rheostat positions.

doi:10.1016/j.bpj.2024.09.013

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Article

Dynamics-based protein network features accurately discriminate neutral and rheostat positions.

Biophysical journal - 15 Oct 2024

Campitelli P, Ross D, Swint-Kruse L, Ozkan S B

Abstract excerpt

In some proteins, a unique class of nonconserved positions is characterized by their ability to generate diverse functional outcomes through single amino acid substitutions. Due to their ability to tune protein function, accurately identifying such "rheostat" positions is crucial for protein design, for understanding the impact of mutations observed in humans, and for predicting the evolution of pathogen drug...

Topics

Molecular Dynamics Simulation
Lac Repressors
Escherichia coli Proteins
Isopropyl Thiogalactoside
Escherichia coli
Allosteric Regulation
Mutation

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Identifiers

PMID: 39277794
DOI: 10.1016/j.bpj.2024.09.013
PMCID: PMC11494493

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026.

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