Evidence map›Paper›PMID 20931264›Full record

ArticleJournal of biomolecular NMR2010

Automated protein resonance assignments of magic angle spinning solid-state NMR spectra of β1 immunoglobulin binding domain of protein G (GB1).

Hunter N B Moseley, Lindsay J Sperling, Chad M Rienstra

Abstract read
In one paragraph

Article in Journal of biomolecular NMR, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed.

  1. Article
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  7. Membrane proteins in their native habitat as seen by solid-state NMR spectroscopy.Protein science : a publication of the Protein Society · 2015
    Review
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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

3 authors.

Hunter N B MoseleyDepartment of Chemistry, University of Louisville, KY 40292, USA. hunter.moseley@louisville.edu
Lindsay J Sperling
Chad M Rienstra

Funding

Structure and Function of Membrane Protein Complexes(RMI)R01GM075937 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI RIENSTRA, CHAD M · 2005 to 2009
$1.4M
NIGMS NIH HHS R01 GM075937NIGMS NIH HHS R01-GM075937
6 · The paper itself

Abstract

Magic-angle spinning solid-state NMR (MAS SSNMR) represents a fast developing experimental technique with great potential to provide structural and dynamics information for proteins not amenable to other methods. However, few automated analysis tools are currently available for MAS SSNMR. We present a methodology for automating protein resonance assignments of MAS SSNMR spectral data and its application to experimental peak lists of the β1 immunoglobulin binding domain of protein G (GB1) derived from a uniformly ¹³C- and ¹⁵N-labeled sample. This application to the 56 amino acid GB1 produced an overall 84.1% assignment of the N, CO, CA, and CB resonances with no errors using peak lists from NCACX 3D, CANcoCA 3D, and CANCOCX 4D experiments. This proof of concept demonstrates the tractability of this problem.

Indexed as

Amino Acid SequenceBinding SitesCarbon IsotopesImmunoglobulinsMolecular Sequence DataNerve Tissue ProteinsNitrogen IsotopesNuclear Magnetic Resonance, BiomolecularProtein BindingProteinsCarbon IsotopesG-substrateImmunoglobulinsNerve Tissue ProteinsNitrogen IsotopesProteins

Identifiers

PMID20931264
PMCPMC2962796

What OpenQuestion holds

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LicenceCC BY-NC
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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.