Evidence map›Paper›PMID 30638530›Full record

ArticleMethods in enzymology2019

Chemical Exchange.

Arthur G Palmer, Hans Koss

Abstract read
In one paragraph

Article in Methods in enzymology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing 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

44 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Activation dynamics of ubiquitin-specific protease 7.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  5. Article
  6. Article
  7. Gating residues govern ligand unbinding kinetics from the buried cavity in HIF-2α PAS-B.Protein science : a publication of the Protein Society · 2024
    Article
  8. Article
  9. Article
  10. Direct Measurement of 8OGbioRxiv : the preprint server for biology · 2024
    Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2023
    Article
  17. Article
  18. Review
  19. Slow conformational changes in the rigid and highly stable chymotrypsin inhibitor 2.Protein science : a publication of the Protein Society · 2023
    Article
  20. Site-based description of RJournal of magnetic resonance (San Diego, Calif. : 1997) · 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.

Arthur G PalmerDepartment of Biochemistry and Molecular Biophysics, Columbia University, New York, NY, United States. Electronic address: agp6@columbia.edu.
Hans KossDepartment of Biochemistry and Molecular Biophysics, Columbia University, New York, NY, United States.

Funding

PROTEIN MOTIONS IN RECOGNITION, REGULATION AND CATALYSISR01GM059273 · NIGMS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI PALMER, ARTHUR G · 1999 to 2018
$5.7M
NIGMS NIH HHS R01 GM059273
6 · The paper itself

Abstract

The phenomenon of chemical or conformational exchange in NMR spectroscopy has enabled detailed characterization of time-dependent aspects of biomolecular function, including folding, molecular recognition, allostery, and catalysis, on timescales from microsecond to second. Importantly, NMR methods based on a variety of spin relaxation parameters have been developed that provide quantitative information on interconversion kinetics, thermodynamic properties, and structural features of molecular states populated to a fraction of a percent at equilibrium and otherwise unobservable by other NMR approaches. The ongoing development of more sophisticated experimental techniques and the necessity to apply these methods to larger and more complex molecular systems engenders a corresponding need for theoretical advances describing such techniques and facilitating data analysis in applications. This review surveys current aspects of the theory of chemical exchange, as utilized in ZZ-exchange; Hahn and Carr-Purcell-Meiboom-Gill (CPMG) spin-echo; and R

Indexed as

Nucleic Acid ConformationProtein ConformationAllosteric RegulationCatalysisMagnetic Resonance SpectroscopyThermodynamicsBloch–McConnellDynamicsKineticsNMR spectroscopySpin relaxation

Identifiers

PMID30638530
PMCPMC7493007

What OpenQuestion holds

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Read underepoch 390

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.