Evidence map›Paper›PMID 32056065›Full record

ArticleJournal of biomolecular NMR2020

Amide additives improve RDC measurements in polyacrylamide.

Talia Fargason, Ting Wang, Naiduwadura Ivon Upekala De Silva, Zihan Zhang, Heather McKelvey, Taylor Knapp, Steve Zaharias, Jun Zhang

Abstract read
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In one paragraph

Article in Journal of biomolecular NMR, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.3field-weighted citation impact, top 47% 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

1 citing paper in PubMed, 4 citations in OpenAlex.

  1. Article
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

8 authors at 1 institution in 1 country.

Talia FargasonDepartment of Chemistry, College of Arts and Sciences, University of Alabama at Birmingham, CH266, 901 14th Street South, Birmingham, AL, 35294-1240, USA.
Ting WangDepartment of Chemistry, College of Arts and Sciences, University of Alabama at Birmingham, CH266, 901 14th Street South, Birmingham, AL, 35294-1240, USA.
Naiduwadura Ivon Upekala De SilvaDepartment of Chemistry, College of Arts and Sciences, University of Alabama at Birmingham, CH266, 901 14th Street South, Birmingham, AL, 35294-1240, USA.
Zihan ZhangDepartment of Chemistry, College of Arts and Sciences, University of Alabama at Birmingham, CH266, 901 14th Street South, Birmingham, AL, 35294-1240, USA.
Heather McKelveyDepartment of Chemistry, College of Arts and Sciences, University of Alabama at Birmingham, CH266, 901 14th Street South, Birmingham, AL, 35294-1240, USA.
Taylor KnappDepartment of Chemistry, College of Arts and Sciences, University of Alabama at Birmingham, CH266, 901 14th Street South, Birmingham, AL, 35294-1240, USA.
Steve ZahariasDepartment of Chemistry, College of Arts and Sciences, University of Alabama at Birmingham, CH266, 901 14th Street South, Birmingham, AL, 35294-1240, USA.
Jun ZhangDepartment of Chemistry, College of Arts and Sciences, University of Alabama at Birmingham, CH266, 901 14th Street South, Birmingham, AL, 35294-1240, USA. zhanguab@uab.edu.ORCID http://orcid.org/0000-0002-5842-7424
University of Alabama at Birmingham · US

Funding

College of Arts and Sciences, University of Alabama at Birmingham (US) Start-up
6 · The paper itself

Abstract

Residual dipolar couplings (RDCs) provide valuable NMR parameters that can be used for structural calculation and verification. Measuring RDCs requires aligning macromolecules using one of various types of alignment media. Of different alignment media options, stretched or compressed polyacrylamide gels are advantageous due to their chemical stability. However, polyacrylamide interacts with proteins and significantly broadens NMR resonances. In this study, we found that the amide-containing compounds asparagine, glutamine and propionamide improve spectral quality of proteins in polyacrylamide gel without significantly reducing the magnitude of RDC values. Moreover, we showed that propionamide is an attractive additive that increases protein solubility without interfering with protein stability, ligand binding or NMR pulse width, suggesting its potential applications for our NMR methods.

Indexed as

Nuclear Magnetic Resonance, BiomolecularAcrylic ResinsPolyacrylamidesAcrylic ResinsPolyacrylamidesAlignment mediumAsparagineGlutaminePropionamideProtein solubilityResidual dipolar couplings

Identifiers

PMID32056065
OpenAlexW3006027649

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.