Pilot corpus: NIH-funded biomedical datasets. Any DOI can be scored on demand — network effects sharpen as coverage grows.

Membrane Proteins Have Distinct Fast Internal Motion and Residual Conformational Entropy

bioRxiv (Cold Spring Harbor Laboratory)(2020)10.1101/2020.04.02.022368Source: DataRank Database

Membrane Proteins Have Distinct Fast Internal Motion and Residual Conformational Entropy is a research paper published in bioRxiv (Cold Spring Harbor Laboratory) (2020). On theSindex it has a DataRank of 0. It has been cited 5 times.

N/A

0DataRank · unranked

Scored on demand from live citation data

Open Access5 citations

Download PDF

Cite:

DataRank reads this dataset's downstream impact straight off the citation graph — no black box, no proprietary weighting. How is this computed?

›Methodology & internals

datarank_citation_only_1hop_v6· scope data_onlyMethodology

Pipeline:MetadataData-paper checkEnrichmentCitation networkScoring

Enrichment:Funding (4 grants)OA: greenTopics (31)IDs (PubMed, OpenAlex)SDGs (1)

FAIR Checklist

Context only (not used in score)

Findable (1/2)

Has DOI

Accessible (1/2)

Open Access

Interoperable (0/2)

Reusable (0/3)

FAIR checklist signals are shown for context only and do not affect DataRank scoring.

Run a calibrated FAIR evaluation for this paper →

We only score data papers we can read in full — never from an abstract alone.

Authors (9)

Brian Fuglestad ORCID,Henry J. Lessen ORCID,Matthew A. Stetz ORCID,Danny W. Lin,Bryan S. Marques

Live enrichment

PubMed:21097893 OpenAlex:https://openalex.org/W3014696633

National Institutes of Health

Grant: 5T32GM008275-04

BIOPHYSICAL SPECTROSCOPY TRAINING PROGRAM

National Institutes of Health

Grant: 5R01GM079440-04

Membrane Protein Stability

National Institutes of Health

Grant: 3P41GM111244-03S1

Life Science and Biomedical technology Research center at NSLS-II LSBR

National Institutes of Health

Grant: 5T32GM008403-22

PROGRAM IN MOLECULAR BIOPHYSICS

greenLicense: cc-by-nc-nd

repositoryhttps://www.biorxiv.org/content/biorxiv/early/2020/04/03/2020.04.02.022368.full.pdf

publisherhttps://syndication.highwire.org/content/doi/10.1101/2020.04.02.022368

repositoryhttps://doi.org/10.1101/2020.04.02.022368

https://onlinelibrary.wiley.com/doi/pdfdirect/10.1002/anie.202003527

Fields of Study

Lipid Membrane Structure and BehaviorProtein Structure and DynamicsPhotoreceptor and optogenetics research0301 basic medicine0303 health sciences03 medical and health sciences

Keywords

ChemistrySide chainConformational entropyIntegral membrane proteinTransmembrane proteinProtein–lipid interactionBiophysicsMembrane proteinMembraneLipid bilayerTransmembrane domainEntropy (arrow of time)Protein structureCrystallographyBiochemistryMoleculeThermodynamicsBiologyPhysicsEntropyMolecular ConformationMembrane ProteinsCrystallography, X-RayNuclear Magnetic Resonance, BiomolecularResearch Articles

Sustainable Development Goals

SDG 0: Clean water and sanitation