Evidence map›Paper›PMID 16373478›Full record

ArticleProtein science : a publication of the Protein Society2006

Protein stabilization by specific binding of guanidinium to a functional arginine-binding surface on an SH3 domain.

Arash Zarrine-Afsar, Anthony Mittermaier, Lewis E Kay, Alan R Davidson

Abstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing 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

22 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Electro-Osmotic Flow Generation via a Sticky Ion Action.bioRxiv : the preprint server for biology · 2023
    Article
  7. How a highly acidic SH3 domain folds in the absence of its charged peptide target.Protein science : a publication of the Protein Society · 2023
    Article
  8. Article
  9. Article
  10. BBA advances · 2022
    Article
  11. Article
  12. Disorder in a two-domain neuronal CaCellular and molecular life sciences : CMLS · 2021
    Article
  13. Article
  14. Article
  15. Reply to Candel et al.: Evidence for evolutionary conservation of folding kinetics in the thioredoxin protein family.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  16. Article
  17. Article
  18. Article
  19. Entropic stabilization of myoglobin by subdenaturing concentrations of guanidine hydrochloride.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2009
    Article
  20. 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.

Arash Zarrine-AfsarDepartment of Biochemistry, University of Toronto, Toronto, Ontario, Canada.
Anthony Mittermaier
Lewis E Kay
Alan R Davidson

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Guanidinium hydrochloride (GuHCl) at low concentrations significantly stabilizes the Fyn SH3 domain. In this work, we have demonstrated that this stabilizing effect is manifested through a dramatic (five- to sixfold) decrease in the unfolding rate of the domain with the folding rate being affected minimally. This behavior contrasts to the effect of NaCl, which stabilizes this domain by accelerating the folding rate. These data imply that the stabilizing effect of GuHCl is not predominantly ionic in nature. Through NMR studies, we have identified a specific binding site for guanidinium, and we have determined a dissociation constant of 90 mM for this interaction. The guanidinium-binding site overlaps with a functionally important arginine-binding pocket on the domain surface, and we have shown that GuHCl is a specific inhibitor of the peptide-binding activity of the domain. A different SH3 domain possessing a similar arginine-binding pocket is also thermodynamically stabilized by GuHCl. These data suggest that many proteins that normally interact with arginine-containing ligands may also be able to specifically interact with guanidinium. Thus, some caution should be used when using GuHCl as a denaturant in protein folding studies. Since arginine-mediated interactions are often important in the energetics of protein-protein interactions, our observations could be relevant for the design of small molecule inhibitors of protein-protein interactions.

Indexed as

AnimalsArginineBinding SitesGuanidineKineticsMagnetic Resonance SpectroscopyMutationPeptidesProtein BindingProtein DenaturationProto-Oncogene Proteins c-fynSodium Chloridesrc Homology DomainsSurface PropertiesThermodynamicsUreaArginineGuanidinePeptidesProto-Oncogene Proteins c-fynSodium ChlorideUrea

Identifiers

PMID16373478
PMCPMC2242360

What OpenQuestion holds

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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.