Evidence map›Paper›PMID 42172735›Full record

ReviewCurrent opinion in structural biology2026

Advancements in single-molecule fluorescence spectroscopy for probing conformations, dynamics, and interactions in disordered protein regions.

Drake Jensen, Jasmine Cubuk, Nirnay Samanta, Melissa D Stuchell-Brereton, Andrea Soranno

Abstract readReview
In one paragraph

Review in Current opinion in structural biology, 2026. 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.

Drake JensenDepartment of Biochemistry and Molecular Biophysics, Washington University in Saint Louis, Saint Louis, 63110, MO, USA; Center for Biomolecular Condensates, Washington University in Saint Louis, Saint Louis, 63130, MO, USA.
Jasmine CubukDepartment of Biochemistry and Molecular Biophysics, Washington University in Saint Louis, Saint Louis, 63110, MO, USA; Center for Biomolecular Condensates, Washington University in Saint Louis, Saint Louis, 63130, MO, USA.
Nirnay SamantaDepartment of Biochemistry and Molecular Biophysics, Washington University in Saint Louis, Saint Louis, 63110, MO, USA; Center for Biomolecular Condensates, Washington University in Saint Louis, Saint Louis, 63130, MO, USA.
Melissa D Stuchell-BreretonDepartment of Biochemistry and Molecular Biophysics, Washington University in Saint Louis, Saint Louis, 63110, MO, USA; Center for Biomolecular Condensates, Washington University in Saint Louis, Saint Louis, 63130, MO, USA.
Andrea SorannoDepartment of Biochemistry and Molecular Biophysics, Washington University in Saint Louis, Saint Louis, 63110, MO, USA; Center for Biomolecular Condensates, Washington University in Saint Louis, Saint Louis, 63130, MO, USA. Electronic address: soranno@wustl.edu.

Funding

A multipronged investigation of SARS-CoV-2 genome packagingR01AI163142 · NIAID · WASHINGTON UNIVERSITY · PI Andrea Soranno · 2022 to 2026
$3.1M
Impact of sequence changes on key intrinsically disordered regions of cardiac troponinR01HL179124 · NHLBI · WASHINGTON UNIVERSITY · PI Michael J Greenberg, Alex S Holehouse · 2025 to 2026
$1.5M
Mechanisms of sigma-factor-dependent transcriptional control in Mycobacterium tuberculosisF32AI186575 · NIAID · WASHINGTON UNIVERSITY · PI Drake Jensen · 2025 to 2026
$155k
NHLBI NIH HHS R01 HL179124NIAID NIH HHS F32 AI186575NIAID NIH HHS R01 AI163142
6 · The paper itself

Abstract

Single-molecule fluorescence spectroscopy encompasses a range of techniques to probe dynamic conformational ensembles of intrinsically disordered regions (IDRs). By resolving subpopulation-specific properties and spanning timescales from nanoseconds to seconds, these measurements provide observables often inaccessible with ensemble measurements. Here, we contextualize key challenges and recent advances, including integrating experiments, simulations, and theory to quantify sequence-encoded effects, as well as photon statistic analyses to characterize protein dynamics. We also summarize extensions of single-molecule fluorescence approaches to decode IDR conformations, dynamics, and spatial organizations within biomolecular condensates. Together, these technical advances make single-molecule fluorescence spectroscopy increasingly accessible for studying IDR function, while the complexity of IDR biology and physics continues to drive further methodological innovation.

Indexed as

Intrinsically Disordered ProteinsSingle Molecule ImagingProtein BindingProtein ConformationSpectrometry, FluorescenceIntrinsically Disordered Proteins

Identifiers

PMID42172735
PMCPMC13359366

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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.