Evidence map›Paper›PMID 34845612›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2022

Labeling of Proteins for Single-Molecule Fluorescence Spectroscopy.

Franziska Zosel, Andrea Holla, Benjamin Schuler

Abstract read
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In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
9.1field-weighted citation impact, top 1% 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

13 citing papers in PubMed, 21 citations in OpenAlex.

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  7. Single-Molecule FRET Analyses of NMDA Receptors.Methods in molecular biology (Clifton, N.J.) · 2024
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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.

Franziska ZoselDepartment of Biochemistry, University of Zurich, Zurich, Switzerland.
Andrea HollaDepartment of Biochemistry, University of Zurich, Zurich, Switzerland.
Benjamin SchulerDepartment of Biochemistry, University of Zurich, Zurich, Switzerland. schuler@bioc.uzh.ch.
University of Zurich · CHNovo Nordisk (Denmark) · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Single-molecule fluorescence spectroscopy has become an important technique for studying the conformational dynamics and folding of proteins. A key step for performing such experiments is the availability of high-quality samples. This chapter describes a simple and widely applicable strategy for preparing proteins that are site-specifically labeled with a donor and an acceptor dye for single-molecule Förster resonance energy transfer (FRET) experiments. The method is based on introducing two cysteine residues that are labeled with maleimide-functionalized fluorophores, combined with high-resolution chromatography. We discuss how to optimize site-specific labeling even in the absence of orthogonal coupling chemistry and present purification strategies that are suitable for samples ranging from intrinsically disordered proteins to large folded proteins. We also discuss common problems in protein labeling, how to avoid them, and how to stringently control sample quality.

Indexed as

Spectrometry, FluorescenceFluorescence Resonance Energy TransferFluorescent DyesIntrinsically Disordered ProteinsSingle Molecule ImagingFluorescent DyesIntrinsically Disordered ProteinsCysteineFluorescence spectroscopyFluorescent dyeFörster resonance energy transferFRETIntrinsically disordered proteinsIon-exchange chromatographyLabelingMaleimideProtein foldingRP-HPLCSingle-molecule detection

Identifiers

PMID34845612
OpenAlexW3215234167

What OpenQuestion holds

Textmetadata
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.