Evidence map›Paper›PMID 21947915›Full record

ArticleJournal of biomolecular NMR2011

The feasibility of parameterizing four-state equilibria using relaxation dispersion measurements.

Pilong Li, Ilídio R S Martins, Michael K Rosen

Abstract read
In one paragraph

Article in Journal of biomolecular NMR, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 citing papers in PubMed.

  1. Ligand-induced protein transition state stabilization switches the binding pathway from conformational selection to induced fit.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  2. Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2023
    Article
  3. Article
  4. Compact expressions for RJournal of magnetic resonance (San Diego, Calif. : 1997) · 2020
    Article
  5. Chemical Exchange.Methods in enzymology · 2019
    Article
  6. Article
  7. Article
  8. General expressions for RJournal of magnetic resonance (San Diego, Calif. : 1997) · 2017
    Article
  9. Article
  10. Visualizing transient dark states by NMR spectroscopy.Quarterly reviews of biophysics · 2015
    Article
  11. Chemical exchange in biomacromolecules: past, present, and future.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2014
    Review
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.

Pilong LiDepartment of Biochemistry and Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390-8816, USA. pilongli@mail.med.upenn.edu
Ilídio R S Martins
Michael K Rosen

Funding

The Pathway to Activation of the Vav Proto-OncogeneR01GM066930 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI ROSEN, MICHAEL K · 2003 to 2006
$1.1M
Howard Hughes Medical InstituteNIGMS NIH HHS GM066930NIGMS NIH HHS R01 GM066930
6 · The paper itself

Abstract

Coupled equilibria play important roles in controlling information flow in biochemical systems, including allosteric molecules and multidomain proteins. In the simplest case, two equilibria are coupled to produce four interconverting states. In this study, we assessed the feasibility of determining the degree of coupling between two equilibria in a four-state system via relaxation dispersion measurements. A major bottleneck in this effort is the lack of efficient approaches to data analysis. To this end, we designed a strategy to efficiently evaluate the smoothness of the target function surface (TFS). Using this approach, we found that the TFS is very rough when fitting benchmark CPMG data to all adjustable variables of the four-state equilibria. After constraining a portion of the adjustable variables, which can often be achieved through independent biochemical manipulation of the system, the smoothness of TFS improves dramatically, although it is still insufficient to pinpoint the solution. The four-state equilibria can be finally solved with further incorporation of independent chemical shift information that is readily available. We also used Monte Carlo simulations to evaluate how well each adjustable parameter can be determined in a large kinetic and thermodynamic parameter space and how much improvement can be achieved in defining the parameters through additional measurements. The results show that in favorable conditions the combination of relaxation dispersion and biochemical manipulation allow the four-state equilibrium to be parameterized, and thus coupling strength between two processes to be determined.

Indexed as

Feasibility StudiesKineticsMagnetic Resonance SpectroscopyModels, MolecularMonte Carlo MethodProteinsThermodynamicsProteins

Identifiers

PMID21947915
PMCPMC3229927

What OpenQuestion holds

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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.