Evidence map›Paper›PMID 24077173›Full record

ReviewMolecules (Basel, Switzerland)2013

Measuring dynamic and kinetic information in the previously inaccessible supra-τ(c) window of nanoseconds to microseconds by solution NMR spectroscopy.

David Ban, T Michael Sabo, Christian Griesinger, Donghan Lee

Abstract readReview
In one paragraph

Review in Molecules (Basel, Switzerland), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

  1. Article
  2. Special Issue "Application of NMR Spectroscopy in Biomolecules".International journal of molecular sciences · 2026
    Article
  3. Article
  4. Review
  5. Deep learning-guided design of dynamic proteins.Science (New York, N.Y.) · 2025
    Article
  6. Article
  7. Probing excited stateMethods (San Diego, Calif.) · 2023
    Article
  8. Article
  9. Article
  10. Arginine Side-Chain Hydrogen Exchange: Quantifying Arginine Side-Chain Interactions in Solution.Chemphyschem : a European journal of chemical physics and physical chemistry · 2019
    Article
  11. Article
  12. Forbidden Coherence Transfer ofMolecules (Basel, Switzerland) · 2017
    Article
  13. Article
  14. Population shuffling between ground and high energy excited states.Protein science : a publication of the Protein Society · 2015
    Article
  15. Article
  16. Article
  17. 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

4 authors.

David BanDepartment for NMR-based Structural Biology, Max-Planck Institute for Biophysical Chemistry, Am Fassberg 11, D-37077 Göttingen, Germany. dole@nmr.mpibpc.mpg.de.
T Michael Sabo
Christian Griesinger
Donghan Lee

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nuclear Magnetic Resonance (NMR) spectroscopy is a powerful tool that has enabled experimentalists to characterize molecular dynamics and kinetics spanning a wide range of time-scales from picoseconds to days. This review focuses on addressing the previously inaccessible supra-tc window (defined as τ(c) < supra-τ(c) < 40 μs; in which tc is the overall tumbling time of a molecule) from the perspective of local inter-nuclear vector dynamics extracted from residual dipolar couplings (RDCs) and from the perspective of conformational exchange captured by relaxation dispersion measurements (RD). The goal of the first section is to present a detailed analysis of how to extract protein dynamics encoded in RDCs and how to relate this information to protein functionality within the previously inaccessible supra-τ(c) window. In the second section, the current state of the art for RD is analyzed, as well as the considerable progress toward pushing the sensitivity of RD further into the supra-τ(c) scale by up to a factor of two (motion up to 25 μs). From the data obtained with these techniques and methodology, the importance of the supra-τ(c) scale for protein function and molecular recognition is becoming increasingly clearer as the connection between motion on the supra-τ(c) scale and protein functionality from the experimental side is further strengthened with results from molecular dynamics simulations.

Indexed as

Molecular Dynamics SimulationNuclear Magnetic Resonance, BiomolecularAlgorithmsKineticsProteinsQuantum TheorySolutionsUbiquitinProteinsSolutionsUbiquitin

Identifiers

PMID24077173
PMCPMC6270068

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Registered trials

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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.