Evidence map›Paper›PMID 28317074›Full record

ReviewJournal of biomolecular NMR2017

Probing conformational dynamics in biomolecules via chemical exchange saturation transfer: a primer.

Pramodh Vallurupalli, Ashok Sekhar, Tairan Yuwen, Lewis E Kay

Abstract readReview
PubMed Publisher
In one paragraph

Review in Journal of biomolecular NMR, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.

0numbers the graph read from it
0cells of the map it votes in
76citing 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

76 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Mapping the FF domain folding pathway via structures of transiently populated folding intermediates.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Direct Measurement of 8OGbioRxiv : the preprint server for biology · 2024
    Article
  18. Exploring Sulfur Sites in Proteins via Triple-ResonanceJournal of the American Chemical Society · 2023
    Article
  19. Article
  20. Probing excited stateMethods (San Diego, Calif.) · 2023
    Article

16 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

4 authors.

Pramodh VallurupalliTIFR Centre for Interdisciplinary Sciences, Hyderabad, India. pramodh@tifrh.res.in.
Ashok SekharDepartments of Molecular Genetics, Biochemistry and Chemistry, University of Toronto, Toronto, ON, Canada.
Tairan YuwenDepartments of Molecular Genetics, Biochemistry and Chemistry, University of Toronto, Toronto, ON, Canada.
Lewis E KayDepartments of Molecular Genetics, Biochemistry and Chemistry, University of Toronto, Toronto, ON, Canada. kay@pound.med.utoronto.ca.ORCID http://orcid.org/0000-0003-3504-7995

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Although Chemical Exchange Saturation Transfer (CEST) type NMR experiments have been used to study chemical exchange processes in molecules since the early 1960s, there has been renewed interest in the past several years in using this approach to study biomolecular conformational dynamics. The methodology is particularly powerful for the study of sparsely populated, transiently formed conformers that are recalcitrant to investigation using traditional biophysical tools, and it is complementary to relaxation dispersion and magnetization transfer experiments that have traditionally been used to study chemical exchange processes. Here we discuss the concepts behind the CEST experiment, focusing on practical aspects as well, we review some of the pulse sequences that have been developed to characterize protein and RNA conformational dynamics, and we discuss a number of examples where the CEST methodology has provided important insights into the role of dynamics in biomolecular function.

Indexed as

Molecular Dynamics SimulationBiopolymersMolecular ConformationNuclear Magnetic Resonance, BiomolecularProteinsRNABiopolymersProteinsRNACESTExcited conformational statesMolecular dynamicsSlow conformational exchange

Identifiers

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.