Evidence map›Paper›PMID 29964175›Full record

ArticleMethods (San Diego, Calif.)2018

Practical aspects of high-pressure NMR spectroscopy and its applications in protein biophysics and structural biology.

José A Caro, A Joshua Wand

Abstract read
In one paragraph

Article in Methods (San Diego, Calif.), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing 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

26 citing papers in PubMed.

  1. Article
  2. Small Molecule Regulation of CLOCK:BMAL1 DNA Binding Activity.bioRxiv : the preprint server for biology · 2026
    Article
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  4. Review
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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

2 authors.

José A CaroJohnson Research Foundation and Department of Biochemistry and Biophysics, University of Pennsylvania Perelman School of Medicine, Philadelphia, PA 19104-6509, United States.
A Joshua WandJohnson Research Foundation and Department of Biochemistry and Biophysics, University of Pennsylvania Perelman School of Medicine, Philadelphia, PA 19104-6509, United States. Electronic address: wand@pennmedicine.upenn.edu.

Funding

STRUCTURAL BIOLOGY TRAINING PROGRAMT32GM008275 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI WAND, A. JOSHUA · 1988 to 2018
$6.0M
STRUCTURAL STUDIES OF CALMODULIN-PEPTIDE COMPLEXESR01DK039806 · NIDDK · UNIVERSITY OF PENNSYLVANIA · PI WAND, A. JOSHUA · 1988 to 2011
$3.5M
STRUCTURE &DYNAMICS OF FREE &COMPLEXED CYTOCHROMES CR01GM035940 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI WAND, A. JOSHUA · 1986 to 2007
$2.8M
Fluctuations and entropy in the energetics and function of protein complexesR01GM102447 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI WAND, A. JOSHUA · 2012 to 2015
$1.4M
NIDDK NIH HHS R01 DK039806NIGMS NIH HHS R01 GM035940NIGMS NIH HHS R01 GM102447NIGMS NIH HHS T32 GM008275
6 · The paper itself

Abstract

Pressure and temperature are the two fundamental variables of thermodynamics. Temperature and chemical perturbation are central experimental tools for the exploration of macromolecular structure and dynamics. Though it has long been recognized that hydrostatic pressure offers a complementary and often unique view of macromolecular structure, stability and dynamics, it has not been employed nearly as much. For solution NMR applications the limited use of high-pressure is undoubtedly traced to difficulties of employing pressure in the context of modern multinuclear and multidimensional NMR. Limitations in pressure tolerant NMR sample cells have been overcome and enable detailed studies of macromolecular energy landscapes, hydration, dynamics and function. Here we review the practical considerations for studies of biological macromolecules at elevated pressure, with a particular emphasis on applications in protein biophysics and structural biology.

Indexed as

Biophysical PhenomenaPressureThermodynamicsNuclear Magnetic Resonance, BiomolecularProtein ConformationProteinsProtein Structure, SecondaryProtein Structure, TertiaryProteinsDynamicsHigh-pressureSolution NMRStructure determinationThermodynamics

Identifiers

PMID29964175
PMCPMC6133745

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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.