Evidence map›Paper›PMID 26352026›Full record

ArticleAngewandte Chemie (International ed. in English)2015

The energetics of a three-state protein folding system probed by high-pressure relaxation dispersion NMR spectroscopy.

Vitali Tugarinov, David S Libich, Virginia Meyer, Julien Roche, G Marius Clore

Abstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed.

  1. Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2023
    Article
  2. Article
  3. Article
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  7. Article
  8. XIPP: multi-dimensional NMR analysis software.Journal of biomolecular NMR · 2020
    Article
  9. How internal cavities destabilize a protein.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  10. Chemical Exchange.Methods in enzymology · 2019
    Article
  11. Lessons from pressure denaturation of proteins.Journal of the Royal Society, Interface · 2018
    Review
  12. A methylJournal of biomolecular NMR · 2018
    Article
  13. Article
  14. Article
  15. Article
  16. 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

5 authors.

Vitali TugarinovLaboratory of Chemical Physics, Building 5, National Institutes of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0520 (USA). vitali.tugarinov@nih.gov.
David S LibichLaboratory of Chemical Physics, Building 5, National Institutes of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0520 (USA).
Virginia MeyerLaboratory of Chemical Physics, Building 5, National Institutes of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0520 (USA).
Julien RocheLaboratory of Chemical Physics, Building 5, National Institutes of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0520 (USA).
G Marius CloreLaboratory of Chemical Physics, Building 5, National Institutes of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0520 (USA). mariusc@mail.nih.gov.

Funding

Structure and Dynamics Of Macromolecules In Solution By NMRZIADK029023 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI CLORE, GIDEON · 2009 to 2025
$41.5M
NMR STUDIES OF THREE-DIMENSIONAL STRUCTURE OF MACROMOLECULES IN SOLUTIONZ01DK029023 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI CLORE, G. MARIUS · 1988 to 2008
$949k
Intramural NIH HHS Z01 DK029023Intramural NIH HHS Z99 DK999999
6 · The paper itself

Abstract

The energetic and volumetric properties of a three-state protein folding system, comprising a metastable triple mutant of the Fyn SH3 domain, have been investigated using pressure-dependent (15) N-relaxation dispersion NMR from 1 to 2500 bar. Changes in partial molar volumes (ΔV) and isothermal compressibilities (ΔκT ) between all the states along the folding pathway have been determined to reasonable accuracy. The partial volume and isothermal compressibility of the folded state are 100 mL mol(-1) and 40 μL mol(-1)  bar(-1) , respectively, higher than those of the unfolded ensemble. Of particular interest are the findings related to the energetic and volumetric properties of the on-pathway folding intermediate. While the latter is energetically close to the unfolded state, its volumetric properties are similar to those of the folded protein. The compressibility of the intermediate is larger than that of the folded state reflecting the less rigid nature of the former relative to the latter.

Indexed as

Nuclear Magnetic Resonance, BiomolecularPressureProtein FoldingProteinsProteinshigh-pressure NMR spectroscopykineticsprotein foldingproteinsrelaxation dispersion

Identifiers

PMID26352026
PMCPMC4692720

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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.