Evidence map›Paper›PMID 33877630›Full record

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

Preparation of a Deuterated Membrane Protein for Small-Angle Neutron Scattering.

Yuqi Wu, Kevin L Weiss, Raquel L Lieberman

Abstract read
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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. Not yet cited in PubMed.

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0cells of the map it votes in
0citing papers in PubMed
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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

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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

3 authors.

Yuqi WuSchool of Chemistry & Biochemistry, Georgia Institute of Technology, Atlanta, GA, USA.
Kevin L WeissNeutron Scattering Division, Oak Ridge National Laboratory, Oak Ridge, TN, USA.
Raquel L LiebermanSchool of Chemistry & Biochemistry, Georgia Institute of Technology, Atlanta, GA, USA. Raquel.Lieberman@chemistry.gatech.edu.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

This chapter outlines a protocol developed to prepare a purified deuterated membrane protein for a small-angle neutron scattering (SANS) experiment. SANS is a noninvasive technique well suited to studying membrane protein solution structures, and deuteration enhances the signal from the protein over the background (Breyton et al., Eur Phys J E Soft Matter 36 (7):71, 2013; Garg et al., Biophys J 101 (2):370-377, 2011). We present our workflow: transformation of our plasmid into E. coli, cell growth and expression of our deuterated protein, membrane isolation, detergent solubilization, protein purification, purity assessment, and final preparation for SANS.

Indexed as

DetergentsEscherichia coliHumansModels, MolecularNeutron DiffractionPlasmidsPresenilinsProtein Structure, SecondaryRecombinant ProteinsScattering, Small AngleTransformation, BacterialWorkflowDetergentsPresenilinsRecombinant ProteinsContrast match pointDetergentDeuterationIntramembrane proteolysisMembrane proteinNeutron scatteringRecombinant expressionα-Helix

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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.