Clustering of Aromatic Amino Acid Residues around Methionine in Proteins.

ABSTRACT: Short-range, non-covalent interactions between amino acid residues determine protein structures and contribute to protein functions in diverse ways. The interactions of the thioether of methionine with the aromatic rings of tyrosine, tryptophan, and/or phenylalanine has long been discussed and such interactions are favorable on the order of 1-3 kcal mol^-1. Here, we carry out a new bioinformatics survey of known protein structures where we assay the propensity of three aromatic residues to localize around the [-CH₂-S-CH₃] of methionine. We term these groups "3-bridge clusters". A dataset consisting of 33,819 proteins with less than 90% sequence identity was analyzed and such clusters were found in 4093 structures (or 12% of the non-redundant dataset). All su

SUBMITTER: Gibbs CA 

PROVIDER: S-EPMC8774105 | biostudies-literature | 2021 Dec

REPOSITORIES: biostudies-literature