Evidence map›Paper›PMID 40494166›Full record

ReviewCurrent opinion in structural biology2025

Capturing protein dynamics across timescales with site-directed spin labeling electron paramagnetic resonance spectroscopy.

Patrick C Brennan, Julian D Grosskopf, Alexander M Garces, Cassandra L Trier, Michael T Lerch

Abstract readReview
In one paragraph

Review in Current opinion in structural biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

5 authors.

Patrick C BrennanDepartment of Biophysics, Medical College of Wisconsin, Milwaukee, WI, USA.
Julian D GrosskopfDepartment of Biophysics, Medical College of Wisconsin, Milwaukee, WI, USA.
Alexander M GarcesDepartment of Biophysics, Medical College of Wisconsin, Milwaukee, WI, USA.
Cassandra L TrierDepartment of Biophysics, Medical College of Wisconsin, Milwaukee, WI, USA.
Michael T LerchDepartment of Biophysics, Medical College of Wisconsin, Milwaukee, WI, USA. Electronic address: mlerch@mcw.edu.

Funding

Development of high-throughput, high-sensitivity EPR sample handling capabilities for biomedical researchR01GM140385 · NIGMS · MEDICAL COLLEGE OF WISCONSIN · PI KLUG, CANDICE S, LERCH, MICHAEL TAYLOR · 2021 to 2024
$1.8M
Regulation of β2-adrenergic receptor signaling by post-translational modificationsR01GM135581 · NIGMS · MEDICAL COLLEGE OF WISCONSIN · PI LERCH, MICHAEL TAYLOR · 2019 to 2023
$1.7M
NIGMS NIH HHS R01 GM135581NIGMS NIH HHS R01 GM140385
6 · The paper itself

Abstract

In the current age of protein structure prediction and determination, resolving the time dependence of structural transitions represents an exciting frontier. Time-resolved biophysical techniques possess the capability to directly observe dynamic structural changes of biomolecules in real time. Here, we review applications of site-directed spin labeling (SDSL) coupled with electron paramagnetic resonance (EPR) spectroscopy that cover a broad range of protein dynamics, from backbone fluctuations on the ps-ns timescale to protein complex assembly formation on the ms-s timescale. Recent developments in SDSL EPR methods allow for direct investigation of protein conformational exchange kinetics on the important μs-ms timescale, providing the time axis for structural transitions needed to define molecular mechanisms of complex biological phenomena.

Indexed as

ProteinsSpin LabelsElectron Spin Resonance SpectroscopyKineticsProtein ConformationProteinsSpin Labels

Identifiers

PMID40494166
PMCPMC12279019

What OpenQuestion holds

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Registered trials

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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.