Evidence map›Paper›PMID 19841630›Full record

ReviewNature chemical biology2009

NMR spectroscopy brings invisible protein states into focus.

Andrew J Baldwin, Lewis E Kay

Abstract readReview
PubMed Publisher
In one paragraph

Review in Nature chemical biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 204 papers.

0numbers the graph read from it
0cells of the map it votes in
204citing papers in PubMed
12.6field-weighted citation impact, top 1% of its field
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

204 citing papers in PubMed, 426 citations in OpenAlex.

  1. Tightly Knotted Enzymes Inhibit Protein-Protein Aggregation.bioRxiv : the preprint server for biology · 2026
    Article
  2. Article
  3. AMIGO - Guided assignment ofJournal of biomolecular NMR · 2026
    Article
  4. Article
  5. Review
  6. Article
  7. Solvation Energetic Costs of Cognate Binding Site Formation.Journal of chemical information and modeling · 2025
    Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Fluorescence-Based Protein Stability Monitoring-A Review.International journal of molecular sciences · 2024
    Review
  16. Article
  17. Genetic switching by the Lac repressor is based on two-state Monod-Wyman-Changeux allostery.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  18. Article
  19. Review
  20. Article

144 more citing papers are in PubMed but not listed here.

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 at 1 institution in 1 country.

Andrew J BaldwinDepartment of Molecular Genetics, The University of Toronto, Toronto, Ontario, Canada.
Lewis E Kay
University of Toronto · CA

Funding

Canadian Institutes of Health Research
6 · The paper itself

Abstract

Molecular dynamics are essential for protein function. In some cases these dynamics involve the interconversion between ground state, highly populated conformers and less populated higher energy structures ('excited states') that play critical roles in biochemical processes. Here we describe recent advances in NMR spectroscopy methods that enable studies of these otherwise invisible excited states at an atomic level and that help elucidate their important relation to function. We discuss a range of examples from molecular recognition, ligand binding, enzyme catalysis and protein folding that illustrate the role that motion plays in 'funneling' conformers along preferred pathways that facilitate their biological function.

Indexed as

CatalysisCytochromes cEnzymesKineticsMagnetic Resonance SpectroscopyModels, MolecularPeptidesPhotochemistryProtein ConformationProtein FoldingProteinsThermodynamicsUbiquitinCytochromes cEnzymesPeptidesProteinsUbiquitin

Identifiers

PMID19841630
OpenAlexW1996859443

What OpenQuestion holds

Textmetadata
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.