Evidence map›Paper›PMID 19581113›Full record

ArticleJournal of magnetic resonance (San Diego, Calif. : 1997)2009

Measurement of one and two bond N-C couplings in large proteins by TROSY-based J-modulation experiments.

Yizhou Liu, James H Prestegard

Abstract read
In one paragraph

Article in Journal of magnetic resonance (San Diego, Calif. : 1997), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing 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

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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

21 citing papers in PubMed.

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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

2 authors.

Yizhou LiuComplex Carbohydrate Research Center, The University of Georgia, Athens, GA 30602, USA.
James H Prestegard

Funding

Sub-project 9U54GM074958 · NIGMS · RUTGERS THE ST UNIV OF NJ NEW BRUNSWICK · PI MONTELIONE, GAETANO T · 2005 to 2009
$56.6M
NMR APPROACHES TO MEMBRANE ASSOCIATED ARF STRUCTURESR01GM061268 · NIGMS · UNIVERSITY OF GEORGIA (UGA) · PI PRESTEGARD, JAMES H. · 2000 to 2014
$2.9M
NIGMS NIH HHS R01 GM061268NIGMS NIH HHS U54 GM074958
6 · The paper itself

Abstract

Residual dipolar couplings (RDCs) between NC' and NC(alpha) atoms in polypeptide backbones of proteins contain information on the orientation of bond vectors that is complementary to that contained in NH RDCs. The (1)J(NC)(alpha) and (2)J(NC)(alpha) scalar couplings between these atoms also display a Karplus relation with the backbone torsion angles and report on secondary structure. However, these N-C couplings tend to be small and they are frequently unresolvable in frequency domain spectra having the broad lines characteristic of large proteins. Here a TROSY-based J-modulated approach for the measurement of small (15)N-(13)C couplings in large proteins is described. The cross-correlation interference effects inherent in TROSY methods improve resolution and signal to noise ratios for large proteins, and the use of J-modulation to encode couplings eliminates the need to remove frequency distortions from overlapping peaks during data analysis. The utility of the method is demonstrated by measurement of (1)J(NC'), (1)J(NC)(alpha) , and (2)J(NC)(alpha) scalar couplings and (1)D(NC') and D(NC)(alpha) residual dipolar couplings for the myristoylated yeast ARF1.GTPgammas protein bound to small lipid bicelles, a system with an effective molecule weight of approximately 70kDa.

Indexed as

ADP-Ribosylation Factor 1AlgorithmsCarbon IsotopesGuanosine 5'-O-(3-Thiotriphosphate)Magnetic Resonance SpectroscopyMyristatesNitrogen IsotopesProteinsSolventsYeastsADP-Ribosylation Factor 1Carbon IsotopesGuanosine 5'-O-(3-Thiotriphosphate)MyristatesNitrogen IsotopesProteinsSolvents

Identifiers

PMID19581113
PMCPMC2763284

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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.