Evidence map›Paper›PMID 33784452›Full record

ArticleBiochemistry2021

Early Strides in NMR Dynamics Measurements.

H Jane Dyson

Abstract readHistorical Article
In one paragraph

Article in Biochemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

1 author.

H Jane DysonDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, United States.ORCID 0000-0001-6855-3398

Funding

Structural Studies of Large Dynamic ComplexesR35GM131693 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI DYSON, HELEN JANE · 2019 to 2023
$2.6M
NIGMS NIH HHS R35 GM131693
6 · The paper itself

Abstract

The study of protein dynamics using the measurement of relaxation times by NMR was based on a set of studies in the mid-20th century that outlined theories and methods. However, the complexity of protein NMR was such that these simple experiments were not practical for application to proteins. The advent of techniques in the 1980s for isotopic labeling of proteins meant that pulse sequences could now be applied in multidimensional NMR experiments to enable per-residue information about the local relaxation times. One of the earliest advances was published in

Indexed as

Crystallography, X-RayHistory, 20th CenturyMicrococcal NucleaseNuclear Magnetic Resonance, BiomolecularProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandMicrococcal Nuclease

Identifiers

PMID33784452
PMCPMC8865369

What OpenQuestion holds

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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.