Evidence map›Paper›PMID 33877592›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2021

Assessing and Improving Protein Sample Quality.

Bertrand Raynal, Sébastien Brûlé, Stephan Uebel, Stefan H Knauer

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In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2021. 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
–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

5 citing papers in PubMed.

  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

4 authors.

Bertrand RaynalPlate-forme de Biophysique Moléculaire, Institut Pasteur, UMR 3528 CNRS, Paris, France.
Sébastien BrûléPlate-forme de Biophysique Moléculaire, Institut Pasteur, UMR 3528 CNRS, Paris, France.
Stephan UebelMax-Planck-Institut für Biochemie, Martinsried, Germany.
Stefan H KnauerBiopolymers, University of Bayreuth, Bayreuth, Germany. stefan.knauer@uni-bayreuth.de.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

One essential prerequisite of any experiment involving a purified protein, such as interaction studies or structural and biophysical characterization, is to work with a "good-quality" sample in order to ensure reproducibility and reliability of the data. Here, we define a "good-quality" sample as a protein preparation that fulfills three criteria: (1) the preparation contains a protein that is pure and soluble and exhibits structural and functional integrity, (2) the protein must be structurally homogeneous, and (3) the preparation must be reproducible. To ensure effective quality control (QC) of all these parameters, we suggest to follow a simple workflow involving the use of gel electrophoresis, light scattering, and spectroscopic experiments. We describe the techniques used in every step of this workflow and provide easy-to-use standard protocols for each step.

Indexed as

Dynamic Light ScatteringElectrophoresis, Polyacrylamide GelMass SpectrometryProteinsProtein StabilityReproducibility of ResultsWorkflowProteinsBatch-to-batch consistencyHomogeneityIdentityOligomeric stateOptimization of storage conditionsProtein stabilityPurityStructural integrity

Identifiers

What OpenQuestion holds

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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.