Evidence map›Paper›PMID 21196937›Full record

ArticleNature structural & molecular biology2011

Site-resolved measurement of water-protein interactions by solution NMR.

Nathaniel V Nucci, Maxim S Pometun, A Joshua Wand

Abstract read
In one paragraph

Article in Nature structural & molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 95 papers.

0numbers the graph read from it
0cells of the map it votes in
95citing 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

95 citing papers in PubMed.

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  14. Slow conformational changes in the rigid and highly stable chymotrypsin inhibitor 2.Protein science : a publication of the Protein Society · 2023
    Article
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35 more citing papers are in PubMed but not listed here.

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.

Nathaniel V NucciJohnson Research Foundation, University of Pennsylvania, Philadelphia, Pennsylvania, USA.
Maxim S Pometun
A Joshua Wand

Funding

NMR Investigation of Protein Hydration and Dynamics under NanoconfinementF32GM087099 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI NUCCI, NATHANIEL V · 2009 to 2011
$144k
NIGMS NIH HHS F32 GM087099NIGMS NIH HHS GM 087099
6 · The paper itself

Abstract

The interactions of biological macromolecules with water are fundamental to their structure, dynamics and function. Historically, characterization of the location and residence times of hydration waters of proteins in solution has been quite difficult. Confining proteins within the nanoscale interior of a reverse micelle slows water dynamics, allowing global protein-water interactions to be detected using nuclear magnetic resonance techniques. Complications that normally arise from hydrogen exchange and long-range dipolar coupling are overcome by the nature of the reverse micelle medium. Characterization of the hydration of ubiquitin demonstrates that encapsulation within a reverse micelle allows detection of dozens of hydration waters. Comparison of nuclear Overhauser effects obtained in the laboratory and rotating frames indicate a considerable range of hydration water dynamics is present on the protein surface. In addition, an unprecedented clustering of different hydration-dynamics classes of sites is evident.

Indexed as

HumansModels, MolecularMolecular Dynamics SimulationNuclear Magnetic Resonance, BiomolecularProteinsSurface-Active AgentsUbiquitinWaterProteinsSurface-Active AgentsUbiquitinWater

Identifiers

PMID21196937
PMCPMC3058360

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.