Evidence map›Paper›PMID 36949673›Full record

ArticleProtein science : a publication of the Protein Society2023

New experimental evidence for pervasive dynamics in proteins.

Erik R P Zuiderweg, David A Case

Abstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Article
  3. New experimental evidence for pervasive dynamics in proteins.Protein science : a publication of the Protein Society · 2023
    Article
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.

Erik R P ZuiderwegRadboud University, Institute for Molecules and Materials, Nijmegen, XZ, 6525, The Netherlands.ORCID 0000-0001-6766-6446
David A CaseRutgers University, Department of Chemistry & Chemical Biology Piscataway, New Jersey, 08854, USA.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

There is ample computational, but only sparse experimental data suggesting that pico-ns motions with 1 Å amplitude are pervasive in proteins in solution. Such motions, if present in reality, must deeply affect protein function and protein entropy. Several NMR relaxation experiments have provided insights into motions of proteins in solution, but they primarily report on azimuthal angle variations of vectors of covalently-linked atoms. As such, these measurements are not sensitive to distance fluctuations, and cannot but under-represent the dynamical properties of proteins. Here we analyze a novel NMR relaxation experiment to measure amide proton transverse relaxation rates in uniformly

Indexed as

ProteinsProtonsEntropyMagnetic Resonance SpectroscopyMolecular Dynamics SimulationNuclear Magnetic Resonance, BiomolecularProteinsProtonscomputationmolecular dynamicsNMR relaxationsidechain motions

Identifiers

PMID36949673
PMCPMC10108438

What OpenQuestion holds

Textmetadata
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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.