Evidence map›Paper›PMID 24656086›Full record

ReviewJournal of magnetic resonance (San Diego, Calif. : 1997)2014

High-resolution NMR spectroscopy of encapsulated proteins dissolved in low-viscosity fluids.

Nathaniel V Nucci, Kathleen G Valentine, A Joshua Wand

Abstract readReview
In one paragraph

Review in Journal of magnetic resonance (San Diego, Calif. : 1997), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
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  11. Article
  12. Article
  13. Article
  14. Entropy in molecular recognition by proteins.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  15. Article
  16. Article
  17. Role of cavities and hydration in the pressure unfolding of T4 lysozyme.Proceedings of the National Academy of Sciences of the United States of America · 2014
    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

3 authors.

Nathaniel V NucciDepartment of Biochemistry and Biophysics, Johnson Research Foundation, University of Pennsylvania Perelman School of Medicine, Philadelphia, PA 19104-6059, USA.
Kathleen G ValentineDepartment of Biochemistry and Biophysics, Johnson Research Foundation, University of Pennsylvania Perelman School of Medicine, Philadelphia, PA 19104-6059, USA.
A Joshua WandDepartment of Biochemistry and Biophysics, Johnson Research Foundation, University of Pennsylvania Perelman School of Medicine, Philadelphia, PA 19104-6059, USA. Electronic address: wand@mail.med.upenn.edu.

Funding

A novel approach to integral & anchored membrane protein structure & functionR01GM085120 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI WAND, A. JOSHUA · 2008 to 2011
$1.5M
Sensitivity enhancement in solution NMR through dynamic nuclear polarizationR21GM107829 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI WAND, A. JOSHUA · 2013 to 2015
$600k
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 GM085120NIGMS NIH HHS GM107829NIGMS NIH HHS R01 GM085120NIGMS NIH HHS R21 GM107829
6 · The paper itself

Abstract

High-resolution multi-dimensional solution NMR is unique as a biophysical and biochemical tool in its ability to examine both the structure and dynamics of macromolecules at atomic resolution. Conventional solution NMR approaches, however, are largely limited to examinations of relatively small (<25kDa) molecules, mostly due to the spectroscopic consequences of slow rotational diffusion. Encapsulation of macromolecules within the protective nanoscale aqueous interior of reverse micelles dissolved in low viscosity fluids has been developed as a means through which the 'slow tumbling problem' can be overcome. This approach has been successfully applied to diverse proteins and nucleic acids ranging up to 100kDa, considerably widening the range of biological macromolecules to which conventional solution NMR methodologies may be applied. Recent advances in methodology have significantly broadened the utility of this approach in structural biology and molecular biophysics.

Indexed as

AlgorithmsAnimalsHumansMicellesNuclear Magnetic Resonance, BiomolecularProteinsSolubilityViscosityMicellesProteinsBiophysicsLow viscosity fluidNucleic acid encapsulationProtein encapsulationReverse micelle NMRStructural biology

Identifiers

PMID24656086
PMCPMC4127067

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.