TY - UNPB
T1 - How sticky are our proteins?
T2 - Quantifying hydrophobicity of the human proteome
AU - Gils, Juami Hermine Mariama van
AU - Gogishvili, Dea
AU - Eck, Jan van
AU - Bouwmeester, Robbin
AU - Dijk, Erik van
AU - Abeln, Sanne
PY - 2021/7/25
Y1 - 2021/7/25
N2 - 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.
AB - 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.
KW - q-bio.BM
M3 - Preprint
VL - 2021
T3 - arXiv
SP - 1
EP - 20
BT - How sticky are our proteins?
ER -