Evidence map›Paper›PMID 26812069›Full record

ArticleJournal of the American Chemical Society2016

A Miniature Protein Stabilized by a Cation-π Interaction Network.

Timothy W Craven, Min-Kyu Cho, Nathaniel J Traaseth, Richard Bonneau, Kent Kirshenbaum

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

20 citing papers in PubMed.

  1. Article
  2. Article
  3. AQcalc: A web server that identifies weak molecular interactions in protein structures.Protein science : a publication of the Protein Society · 2023
    Article
  4. Design and Engineering of Miniproteins.ACS bio & med chem Au · 2022
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Cation-π binding ability of BN indole.Chemical communications (Cambridge, England) · 2020
    Article
  13. Secondary Forces in Protein Folding.ACS chemical biology · 2019
    Review
  14. Amorphous AgiScience · 2019
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. 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

5 authors.

Timothy W CravenDepartment of Chemistry, New York University , 100 Washington Square East, New York, New York 10003, United States.
Min-Kyu ChoDepartment of Chemistry, New York University , 100 Washington Square East, New York, New York 10003, United States.
Nathaniel J TraasethDepartment of Chemistry, New York University , 100 Washington Square East, New York, New York 10003, United States.
Richard BonneauDepartment of Biology, Center for Genomics and Systems Biology, New York University , 12 Waverly Place, New York, New York 10003, United States.
Kent KirshenbaumDepartment of Chemistry, New York University , 100 Washington Square East, New York, New York 10003, United States.

Funding

Mechanisms of Allostery and Molecular Recognition in the Small Multidrug Resistance FamilyR01AI108889 · NIAID · NEW YORK UNIVERSITY · PI Nathaniel J. Traaseth · 2014 to 2026
$5.4M
Acquisition of a Cryoprobe for a 600 MHz NMR SpectrometerS10OD016343 · OD · NEW YORK UNIVERSITY · PI KROGSGAARD, MICHELLE, TRAASETH, NATHANIEL J. · 2014 to 2014
$360k
NIAID NIH HHS R01 AI108889NIAID NIH HHS R01AI108889NIH HHS S10 OD016343NIH HHS S10OD016343
6 · The paper itself

Abstract

The design of folded miniature proteins is predicated on establishing noncovalent interactions that direct the self-assembly of discrete thermostable tertiary structures. In this work, we describe how a network of cation-π interactions present in proteins containing "WSXWS motifs" can be emulated to stabilize the core of a miniature protein. This 19-residue protein sequence recapitulates a set of interdigitated arginine and tryptophan residues that stabilize a distinctive β-strand:loop:PPII-helix topology. Validation of the compact fold determined by NMR was carried out by mutagenesis of the cation-π network and by comparison to the corresponding disulfide-bridged structure. These results support the involvement of a coordinated set of cation-π interactions that stabilize the tertiary structure.

Indexed as

Amino Acid MotifsAmino Acid SequenceCationsMolecular Sequence DataNuclear Magnetic Resonance, BiomolecularProteinsProtein Structure, TertiarySequence AlignmentCationsProteins

Identifiers

PMID26812069
PMCPMC4867217

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.