Evidence map›Paper›PMID 33389765›Full record

ArticleProtein science : a publication of the Protein Society2021

A systematic analysis of the beta hairpin motif in the Protein Data Bank.

Cory D DuPai, Bryan W Davies, Claus O Wilke

Abstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing 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

18 citing papers in PubMed.

  1. Article
  2. Self-Assembly of Peptides and Biomolecular Systems Into Functional Nanomaterials.Journal of peptide science : an official publication of the European Peptide Society · 2026
    Review
  3. Article
  4. Article
  5. Barrel expansion of outer membrane protein G nanopore through β-hairpin duplication.Protein science : a publication of the Protein Society · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. A Perspective on the (Rise and Fall of) Protein β-Turns.International journal of molecular sciences · 2022
    Review
  15. Article
  16. Article
  17. Current Approaches in Supersecondary Structures Investigation.International journal of molecular sciences · 2021
    Review
  18. A systematic analysis of the beta hairpin motif in the Protein Data Bank.Protein science : a publication of the Protein Society · 2021
    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

3 authors.

Cory D DuPaiDepartment of Molecular Biosciences, University of Texas at Austin, Austin, Texas, USA.ORCID 0000-0002-7915-9473
Bryan W DaviesDepartment of Molecular Biosciences, University of Texas at Austin, Austin, Texas, USA.ORCID 0000-0002-2046-0341
Claus O WilkeDepartment of Integrative Biology, University of Texas at Austin, Austin, Texas, USA.ORCID 0000-0002-7470-9261

Funding

Investigating nanobodies to target multidrug resistant bacterial pathogensR01AI148419 · NIAID · UNIVERSITY OF TEXAS AT AUSTIN · PI DAVIES, BRYAN WILLIAM · 2020 to 2023
$2.8M
A High-Throughput Molecular Platform for Antimicrobial Discovery and StudyR01AI125337 · NIAID · UNIVERSITY OF TEXAS AT AUSTIN · PI DAVIES, BRYAN WILLIAM · 2016 to 2020
$2.0M
NIAID NIH HHS R01 AI125337NIAID NIH HHS R01 AI148419
6 · The paper itself

Abstract

The beta hairpin motif is a ubiquitous protein structural motif that can be found in molecules across the tree of life. This motif, which is also popular in synthetically designed proteins and peptides, is known for its stability and adaptability to broad functions. Here, we systematically probe all 49,000 unique beta hairpin substructures contained within the Protein Data Bank (PDB) to uncover key characteristics correlated with stable beta hairpin structure, including amino acid biases and enriched interstrand contacts. We find that position specific amino acid preferences, while seen throughout the beta hairpin structure, are most evident within the turn region, where they depend on subtle turn dynamics associated with turn length and secondary structure. We also establish a set of broad design principles, such as the inclusion of aspartic acid residues at a specific position and the careful consideration of desired secondary structure when selecting residues for the turn region, that can be applied to the generation of libraries encoding proteins or peptides containing beta hairpin structures.

Indexed as

Amino Acid MotifsDatabases, ProteinProteinsAmino Acid SequenceComputational BiologyProteinsbeta hairpincomputational biologyPDBprotein design

Identifiers

PMID33389765
PMCPMC7888580

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.