Evidence map›Paper›PMID 31915980›Full record

ArticleJournal of biomolecular NMR2020

Two-dimensional NMR lineshape analysis of single, multiple, zero and double quantum correlation experiments.

Christopher A Waudby, Margaux Ouvry, Ben Davis, John Christodoulou

Abstract read
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 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing 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

9 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

4 authors.

Christopher A WaudbyInstitute of Structural and Molecular Biology, University College London and Birkbeck College, London, UK. c.waudby@ucl.ac.uk.ORCID http://orcid.org/0000-0001-7810-3753
Margaux OuvryBiotechnologie, Sanofi, Route d'Avignon, 30390, Aramon, France.
Ben DavisVernalis (R&D) Limited, Granta Park, Great Abington, UK.
John ChristodoulouInstitute of Structural and Molecular Biology, University College London and Birkbeck College, London, UK.ORCID https://orcid.org/0000-0002-6710-3843

Funding

Medical Research Council MC_U117533887Wellcome Trust 206409/Z/17/ZWellcome Trust FC001029
6 · The paper itself

Abstract

NMR spectroscopy provides a powerful approach for the characterisation of chemical exchange and molecular interactions by analysis of series of experiments acquired over the course of a titration measurement. The appearance of NMR resonances undergoing chemical exchange depends on the frequency difference relative to the rate of exchange, and in the case of one-dimensional experiments chemical exchange regimes are well established and well known. However, two-dimensional experiments present additional complexity, as at least one additional frequency difference must be considered. Here we provide a systematic classification of chemical exchange regimes in two-dimensional NMR spectra. We highlight important differences between exchange in HSQC and HMQC experiments, that on a practical level result in more severe exchange broadening in HMQC spectra, but show that complementary alternatives to the HMQC are available in the form of HZQC and HDQC experiments. We present the longitudinal relaxation optimised SOFAST-H(Z/D)QC experiment for the simultaneous acquisition of sensitivity-enhanced HZQC and HDQC spectra, and the longitudinal and transverse relaxation optimised BEST-ZQ-TROSY for analysis of large molecular weight systems. We describe the application of these experiments to the characterisation of the interaction between the Hsp90 N-terminal domain and a small molecule ligand, and show that the independent analysis of HSQC, HMQC, HZQC and HDQC experiments provides improved confidence in the fitted dissociation constant and dissociation rate. Joint analysis of such data may provide improved sensitivity to detect and analyse more complex multi-state interaction mechanisms such as induced fit or conformational selection.

Indexed as

AlgorithmsNuclear Magnetic Resonance, BiomolecularQuantum TheoryHSP90 Heat-Shock ProteinsLigandsProtein BindingProtein DomainsHSP90 Heat-Shock ProteinsLigandsChemical exchangeDouble-quantumLineshape analysisMultiple-quantumTitrationsTwo-dimensional NMRZero-quantum

Identifiers

PMID31915980
PMCPMC7015968

What OpenQuestion holds

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LicenceCC BY
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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.