Evidence map›Paper›PMID 35921001›Full record

ArticleJournal of biomolecular NMR2022

The measurement of binding affinities by NMR chemical shift perturbation.

Billy Hobbs, Jack Drant, Mike P Williamson

Abstract read
In one paragraph

Article in Journal of biomolecular NMR, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Formulation insights into competitive binding of NJournal of pharmaceutical and biomedical analysis · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Protein Binding: A Fuzzy Concept.Life (Basel, Switzerland) · 2023
    Article
  12. Article
  13. 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.

Billy HobbsSchool of Biosciences, University of Sheffield, Firth Court, Western Bank, Sheffield, S10 2TN, UK.
Jack DrantSchool of Biosciences, University of Sheffield, Firth Court, Western Bank, Sheffield, S10 2TN, UK.
Mike P WilliamsonSchool of Biosciences, University of Sheffield, Firth Court, Western Bank, Sheffield, S10 2TN, UK. m.williamson@sheffield.ac.uk.ORCID http://orcid.org/0000-0001-5572-1903

Funding

Biotechnology and Biological Sciences Research Council BB/R000727/1Engineering and Physical Sciences Research Council EP/S01358X/1
6 · The paper itself

Abstract

We have carried out chemical shift perturbation titrations on three contrasting proteins. The resulting chemical shifts have been analysed to determine the best way to fit the data, and it is concluded that a simultaneous fitting of all raw shift data to a single dissociation constant is both the most accurate and the most precise method. It is shown that the optimal weighting of

Indexed as

Magnetic Resonance ImagingProteinsLigandsMagnetic Resonance SpectroscopyNuclear Magnetic Resonance, BiomolecularProtein BindingLigandsProteinsAffinityBindingChemical shiftConformational changeDissociation constantNMR

Identifiers

PMID35921001
PMCPMC9427925

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.