Evidence map›Paper›PMID 19280122›Full record

ArticleJournal of biomolecular NMR2009

Differences in lysine pKa values may be used to improve NMR signal dispersion in reductively methylated proteins.

Sherwin J Abraham, Tomoyoshi Kobayashi, R John Solaro, Vadim Gaponenko

Open access · greenAbstract read
In one paragraph

Article in Journal of biomolecular NMR, 2009. 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
0.8field-weighted citation impact, top 28% 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. Heteromerization of chemokine (C-X-C motif) receptor 4 with α1A/B-adrenergic receptors controls α1-adrenergic receptor function.Proceedings of the National Academy of Sciences of the United States of America · 2015
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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 at 1 institution in 1 country.

Sherwin J AbrahamDepartment of Biochemistry and Molecular Genetics, University of Illinois at Chicago, Chicago, IL 60607, USA.
Tomoyoshi Kobayashi
R John Solaro
Vadim Gaponenko
University of Illinois Chicago · US

Funding

Sarcomeric Modifications and Progressive Cardiac MaladaptationP01HL062426 · NHLBI · UNIVERSITY OF ILLINOIS AT CHICAGO · PI SOLARO, R JOHN · 2000 to 2020
$42.4M
900MHz NMR for Structural Biology in ChicagoP41GM068944 · NIGMS · UNIVERSITY OF ILLINOIS AT CHICAGO · PI GETTINS, PETER G.W. · 2003 to 2007
$6.2M
Design of Therapeutic Peptide-Based NanoparticlesR01CA135341 · NCI · UNIVERSITY OF ILLINOIS AT CHICAGO · PI GAPONENKO, VADIM V · 2010 to 2014
$1.5M
Molecular Mechanism of Troponin Function in Health and DiseaseR01HL082923 · NHLBI · UNIVERSITY OF ILLINOIS AT CHICAGO · PI KOBAYASHI, TOMOYOSHI · 2006 to 2009
$1.1M
NCI NIH HHS R01 CA135341NHLBI NIH HHS P01 HL062426NHLBI NIH HHS P01HL62426NHLBI NIH HHS R01 HL082923NHLBI NIH HHS R01HL082923NIGMS NIH HHS P41 GM068944NIGMS NIH HHS P41 GM68944
6 · The paper itself

Abstract

Reductive methylation of lysine residues in proteins offers a way to introduce 13C methyl groups into otherwise unlabeled molecules. The 13C methyl groups on lysines possess favorable relaxation properties that allow highly sensitive NMR signal detection. One of the major limitations in the use of reductive methylation in NMR is the signal overlap of 13C methyl groups in NMR spectra. Here we show that the uniform influence of the solvent on chemical shifts of exposed lysine methyl groups could be overcome by adjusting the pH of the buffering solution closer to the pKa of lysine side chains. Under these conditions, due to variable pKa values of individual lysine side chains in the protein of interest different levels of lysine protonation are observed. These differences are reflected in the chemical shift differences of methyl groups in reductively methylated lysines. We show that this approach is successful in four different proteins including Ca2+-bound Calmodulin, Lysozyme, Ca2+-bound Troponin C, and Glutathione S-Transferase. In all cases significant improvement in NMR spectral resolution of methyl signals in reductively methylated proteins was obtained. The increased spectral resolution helps with more precise characterization of protein structural rearrangements caused by ligand binding as shown by studying binding of Calmodulin antagonist trifluoperazine to Calmodulin. Thus, this approach may be used to increase resolution in NMR spectra of 13C methyl groups on lysine residues in reductively methylated proteins that enhances the accuracy of protein structural assessment.

Indexed as

Nuclear Magnetic Resonance, BiomolecularCalciumCalmodulinCarbon IsotopesGlutathione TransferaseHydrogen-Ion ConcentrationIsoelectric PointLysineMethylationModels, MolecularMuramidaseProtein ConformationProteinsTroponin CCalciumCalmodulinCarbon IsotopesGlutathione TransferaseLysineMuramidaseProteinsTroponin C

Identifiers

PMID19280122
PMCPMC2736131
OpenAlexW2090169174

What OpenQuestion holds

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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.