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A parametrized two-domain thermodynamic model explains diverse mutational effects on protein allostery

bioRxiv (Cold Spring Harbor Laboratory)(2023)10.1101/2023.08.06.552196Source: DataRank Database

A parametrized two-domain thermodynamic model explains diverse mutational effects on protein allostery is a research paper published in bioRxiv (Cold Spring Harbor Laboratory) (2023). On theSindex it has a DataRank of 0. It has been cited 1 time.

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Enrichment:Funding (2 grants)OA: greenTopics (21)IDs (PubMed)

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Authors (4)

Thomas Gillis ORCID,Srivatsan Raman ORCID,Qiang Cui ORCID,Zhuang Liu ORCID

Live enrichment

PubMed:37662419

National Institutes of Health

Grant: 5R35GM141930-02

Computational Analysis of Enzyme Catalysis and Regulation

National Institutes of Health

Grant: 1DP2GM132682-01

Understanding molecular rules governing protein allostery by deep mutational scanning

greenLicense: cc-by-nd

repositoryhttps://www.biorxiv.org/content/biorxiv/early/2023/08/26/2023.08.06.552196.full.pdf

publisherhttps://syndication.highwire.org/content/doi/10.1101/2023.08.06.552196

repositoryhttps://pmc.ncbi.nlm.nih.gov/articles/PMC10473640/pdf/nihpp-2023.08.06.552196v3.pdf

https://doi.org/10.7554/elife.92262.2

https://doi.org/10.7554/elife.92262

Fields of Study

0301 basic medicine03 medical and health sciences

Keywords

epistasisModels, Molecularthermodynamic modelallosteryQH301-705.5ScienceStructural Biology and Molecular BiophysicsBayesian inferenceQRallosteric hotspotsArticleRepressor ProteinsAllosteric RegulationProtein DomainsMutationMedicineThermodynamicsBiology (General)