Evidence map›Paper›PMID 36699344›Full record

ArticleBioinformatics advances2022

How sticky are our proteins? Quantifying hydrophobicity of the human proteome.

Juami Hermine Mariama van Gils, Dea Gogishvili, Jan van Eck, Robbin Bouwmeester, Erik van Dijk, Sanne Abeln

Abstract read
In one paragraph

Article in Bioinformatics advances, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed.

  1. Article
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  9. Plasmonic Single-Molecule Affinity Detection at 10Advanced materials (Deerfield Beach, Fla.) · 2025
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  10. Article
  11. Electric Field Cycling of Physisorbed Antibodies Reduces Biolayer Polarization Dispersion.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  12. Article
  13. Review
  14. Article
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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

6 authors.

Juami Hermine Mariama van GilsComputer Science Department, Center for Integrative Bioinformatics (IBIVU), Vrije Universiteit Amsterdam, 1081 HV Noord-Holland, The Netherlands.ORCID https://orcid.org/0000-0003-3706-7818
Dea GogishviliComputer Science Department, Center for Integrative Bioinformatics (IBIVU), Vrije Universiteit Amsterdam, 1081 HV Noord-Holland, The Netherlands.
Jan van EckComputer Science Department, Center for Integrative Bioinformatics (IBIVU), Vrije Universiteit Amsterdam, 1081 HV Noord-Holland, The Netherlands.
Robbin BouwmeesterComputer Science Department, Center for Integrative Bioinformatics (IBIVU), Vrije Universiteit Amsterdam, 1081 HV Noord-Holland, The Netherlands.
Erik van DijkComputer Science Department, Center for Integrative Bioinformatics (IBIVU), Vrije Universiteit Amsterdam, 1081 HV Noord-Holland, The Netherlands.
Sanne AbelnComputer Science Department, Center for Integrative Bioinformatics (IBIVU), Vrije Universiteit Amsterdam, 1081 HV Noord-Holland, The Netherlands.ORCID https://orcid.org/0000-0002-2779-7174

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Summary: Proteins tend to bury hydrophobic residues inside their core during the folding process to provide stability to the protein structure and to prevent aggregation. Nevertheless, proteins do expose some 'sticky' hydrophobic residues to the solvent. These residues can play an important functional role, e.g. in protein-protein and membrane interactions. Here, we first investigate how hydrophobic protein surfaces are by providing three measures for surface hydrophobicity: the total hydrophobic surface area, the relative hydrophobic surface area and-using our MolPatch method-the largest hydrophobic patch. Secondly, we analyze how difficult it is to predict these measures from sequence: by adapting solvent accessibility predictions from NetSurfP2.0, we obtain well-performing prediction methods for the THSA and RHSA, while predicting LHP is more challenging. Finally, we analyze implications of exposed hydrophobic surfaces: we show that hydrophobic proteins typically have low expression, suggesting cells avoid an overabundance of sticky proteins. Availability and implementation: The data underlying this article are available in GitHub at https://github.com/ibivu/hydrophobic_patches. Supplementary information: Supplementary data are available at

Identifiers

PMID36699344
PMCPMC9710682

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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.