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Integrating single-molecule spectroscopy and simulations for the study of intrinsically disordered proteins

Methods(2021)10.1016/j.ymeth.2021.03.018Source: DataRank Database

Integrating single-molecule spectroscopy and simulations for the study of intrinsically disordered proteins is a research paper published in Methods (2021). On theSindex it has a DataRank of 0. It has been cited 34 times.

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Open Access34 citations

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Enrichment:Funding (5 grants)OA: greenTopics (20)IDs (PubMed, PMC)Annotations (1)

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Findable (1/2)

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Accessible (1/2)

Open Access

Interoperable (0/2)

Reusable (0/3)

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Authors (3)

Andrea Soranno ORCID,Alex S. Holehouse ORCID,Jhullian J. Alston ORCID

Live enrichment

PubMed:33831596 PMC:PMC8713295

NIGMS NIH HHS

Grant: R25 GM103757

NIA NIH HHS

Grant: R01 AG062837

National Institutes of Health

Grant: 5R25GM103757-08

MAXIMIZING STUDENT DIVERSITY IN THE BIOMEDICAL SCIENCES AT WASHINGTON UNIVERSITY

National Institutes of Health

Grant: 5R01AG062837-04

Conformational and functional analysis of Apolipoprotein E

NIH

greenLicense: cc-by-nc-nd

repositoryhttps://www.ncbi.nlm.nih.gov/pmc/articles/8713295

publisherhttps://api.elsevier.com/content/article/PII:S104620232100092X?httpAccept=text/xml

publisherhttps://api.elsevier.com/content/article/PII:S104620232100092X?httpAccept=text/plain

Europe_PMChttps://europepmc.org/articles/PMC8713295

Europe_PMChttps://europepmc.org/articles/PMC8713295?pdf=render

Fields of Study

0301 basic medicine0303 health sciences03 medical and health sciences

MeSH Terms

Fluorescence Resonance Energy TransferProtein ConformationIntrinsically Disordered ProteinsSingle Molecule Imaging

Keywords

Protein foldingFRETFörster Resonance Energy TransferFluorescence Correlation SpectroscopyIntrinsically Disordered ProteinsMolecular SimulationsSingle-molecule SpectroscopySmfretAll-atom SimulationsProtein ConformationFluorescence Resonance Energy TransferArticleSingle Molecule Imaging