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

Research output: Contribution to JournalArticleAcademic

12 Downloads (Pure)

Abstract

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, for example in protein-protein and membrane interactions. Here, we 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 analyse 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 difficult. Finally, we analyse implications of exposed hydrophobic surfaces: we show that hydrophobic proteins typically have low expression, suggesting cells avoid an overabundance of sticky proteins.
Original languageEnglish
Pages (from-to)1-20
Number of pages20
JournalarXiv.org
Volume2021
Publication statusPublished - 25 Jul 2021

Keywords

  • q-bio.BM

Fingerprint

Dive into the research topics of 'How sticky are our proteins? Quantifying hydrophobicity of the human proteome'. Together they form a unique fingerprint.

Cite this