Evidence map›Paper›PMID 32159932›Full record

ArticleCurrent protocols in chemical biology2020

Ratiometric Single-Molecule FRET Measurements to Probe Conformational Subpopulations of Intrinsically Disordered Proteins.

Irem Nasir, Emily P Bentley, Ashok A Deniz

Open access · hybridAbstract read
In one paragraph

Article in Current protocols in chemical biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
1.8field-weighted citation impact, top 13% 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

3 citing papers in PubMed, 8 citations in OpenAlex.

  1. Article
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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 2 institutions in 2 countries.

Irem NasirDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, California.
Emily P BentleyDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, California.
Ashok A DenizDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, California.
Scripps Research Institute · USChalmers University of Technology · SE

Funding

Single Molecule Studies of Protein Folding MechanismsR01GM066833 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI DENIZ, ASHOK A · 2003 to 2017
$5.2M
Molecular basis for regulation of CREB by cell stress and retroviral oncoproteinsR01CA214054 · NCI · SCRIPPS RESEARCH INSTITUTE, THE · PI DENIZ, ASHOK A, WRIGHT, PETER EDWIN · 2017 to 2021
$3.0M
Biophysics of Protein Disorder and Complexity, Single Molecules to MesoscalesR35GM130375 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI DENIZ, ASHOK A · 2019 to 2023
$2.4M
NCI NIH HHS R01 CA214054NIGMS NIH HHS R01 GM066833NIGMS NIH HHS R35 GM130375
6 · The paper itself

Abstract

Over the past few decades, numerous examples have demonstrated that intrinsic disorder in proteins lies at the heart of many vital processes, including transcriptional regulation, stress response, cellular signaling, and most recently protein liquid-liquid phase separation. The so-called intrinsically disordered proteins (IDPs) involved in these processes have presented a challenge to the classic protein "structure-function paradigm," as their functions do not necessarily involve well-defined structures. Understanding the mechanisms of IDP function is likewise challenging because traditional structure determination methods often fail with such proteins or provide little information about the diverse array of structures that can be related to different functions of a single IDP. Single-molecule fluorescence methods can overcome this ensemble-average masking, allowing the resolution of subpopulations and dynamics and thus providing invaluable insights into IDPs and their function. In this protocol, we describe a ratiometric single-molecule Förster resonance energy transfer (smFRET) routine that permits the investigation of IDP conformational subpopulations and dynamics. We note that this is a basic protocol, and we provide brief information and references for more complex analysis schemes available for in-depth characterization. This protocol covers optical setup preparation and protein handling and provides insights into experimental design and outcomes, together with background information about theory and a brief discussion of troubleshooting. © 2020 by John Wiley & Sons, Inc. Basic Protocol: Ratiometric smFRET detection and analysis of IDPs Support Protocol 1: Fluorophore labeling of a protein through maleimide chemistry Support Protocol 2: Sample chamber preparation Support Protocol 3: Determination of direct excitation of acceptor by donor excitation and leakage of donor emission to acceptor emission channel.

Indexed as

Fluorescence Resonance Energy TransferFluorescent DyesIntrinsically Disordered ProteinsProtein ConformationSingle Molecule ImagingFluorescent DyesIntrinsically Disordered Proteinsconformational dynamicsconformational landscapesintrinsically disordered proteinssingle-molecule fluorescencesmFRET

Identifiers

PMID32159932
PMCPMC7508418
OpenAlexW3011755993

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.