title: Surface accessibility of protein post-translational modifications.
abstract: Protein post-translational modifications are crucial to the function of many proteins. In this study, we have investigated the structural environment of 8378 incidences of 44 types of post-translational modifications with 19 different approaches. We show that modified amino acids likely to be involved in protein-protein interactions, such as ester-linked phosphorylation, methylarginine, acetyllysine, sulfotyrosine, hydroxyproline, and hydroxylysine, are clearly surface associated. Other modifications, including O-GlcNAc, phosphohistidine, 4-aspartylphosphate, methyllysine, and ADP-ribosylarginine, are either not surface associated or are in a protein's core. Artifactual modifications were found to be randomly distributed throughout the protein. We discuss how the surface accessibility of post-translational modifications can be important for protein-protein interactivity.
authors.affiliation: Systems Biology Group, School of Biotechnology and Biomolecular Sciences, University of New South Wales, Sydney, NSW, Australia.
authors.forename: Chi Nam Ignatius
authors.initials: CN
authors.lastname: Pang
authors.forename: Andrew
authors.initials: A
authors.lastname: Hayen
authors.forename: Marc Ronald
authors.initials: MR
authors.lastname: Wilkins
mesh_terms: D000596:Amino Acids / Q000737:chemistry*; D030562:Databases, Protein; D011499:Protein Processing, Post-Translational; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D013499:Surface Properties
chemical_list: D000596:Amino Acids; D011506:Proteins