Evidence map›Paper›PMID 36165617›Full record

ArticlePhysical chemistry chemical physics : PCCP2022

Confinement dependence of protein-associated solvent dynamics around different classes of proteins, from the EPR spin probe perspective.

Wei Li, Katie Lynn Whitcomb, Kurt Warncke

Open access · greenAbstract read
In one paragraph

Article in Physical chemistry chemical physics : PCCP, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.5field-weighted citation impact, top 38% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

5 citing papers in PubMed, 7 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Wei LiDepartment of Physics, Emory University, Atlanta, Georgia, 30322. kwarncke@physics.emory.edu.ORCID http://orcid.org/0000-0001-7319-5628
Katie Lynn WhitcombDepartment of Physics, Emory University, Atlanta, Georgia, 30322. kwarncke@physics.emory.edu.
Kurt WarnckeDepartment of Physics, Emory University, Atlanta, Georgia, 30322. kwarncke@physics.emory.edu.ORCID http://orcid.org/0000-0002-3587-3720
Emory University · US

Funding

Co(II) Radical Pair Dynamics in B12 Enzyme CatalysisR01GM142113 · NIGMS · EMORY UNIVERSITY · PI WARNCKE, KURT · 2020 to 2023
$1.3M
Electron Paramagnetic Resonance SpectrometerS10RR017767 · NCRR · EMORY UNIVERSITY · PI WARNCKE, KURT · 2003 to 2003
$261k
NCRR NIH HHS S10 RR017767NIGMS NIH HHS R01 GM142113
6 · The paper itself

Abstract

Protein function is modulated by coupled solvent fluctuations, subject to the degree of confinement from the surroundings. To identify universal features of the external confinement effect, the temperature dependence of the dynamics of protein-associated solvent over 200-265 K for proteins representative of different classes and sizes is characterized by using the rotational correlation time (detection bandwidth, 10

Indexed as

Ethanolamine Ammonia-LyaseIntrinsically Disordered ProteinsCaseinsDimethyl SulfoxideElectron Spin Resonance SpectroscopyIceMyoglobinProtaminesSolventsSpin LabelsStreptavidinWaterCaseinsDimethyl SulfoxideEthanolamine Ammonia-LyaseIceIntrinsically Disordered ProteinsMyoglobinProtaminesSolventsSpin LabelsStreptavidinWater

Identifiers

PMID36165617
PMCPMC10371532
OpenAlexW4297260148

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

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.