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biomoleculesArticleClustering of Aromatic Amino Acid Residues close to Methionine in ProteinsCurtis A. Gibbs , David S. Weber and Jeffrey J. Warren Division of Chemistry, Simon Fraser University, 8888 University Drive, Burnaby, BC V5A 1S6, Canada; [email protected] (C.A.G.); [email protected] (D.S.W.) Correspondence: [email protected] These authors contributed equally.Abstract: Short-range, non-covalent interactions in between amino acid residues decide protein structures and contribute to protein functions in diverse ways. The interactions of the thioether of methionine using the aromatic rings of tyrosine, tryptophan, and/or phenylalanine has lengthy been talked about and such interactions are favorable about the buy of one kcal mol-1 . Right here, we carry out a brand new bioinformatics survey of acknowledged protein structures the place we assay the propensity of 3 aromatic residues to localize close to the [-CH2 -S-CH3 ] of methionine. We phrase these groups “3-bridge clusters”. A dataset consisting of 33,819 proteins with lower than 90 sequence identity was analyzed and this kind of clusters had been located in 4093 structures (or twelve of the non-redundant dataset). All sub-classes of enzymes have been represented. A 3D coordinate evaluation exhibits that the majority aromatic groups localize near the CH2 and CH3 of methionine. Quantum chemical calculations assistance that the 3-bridge clusters involve a network of interactions that involve the Met-S, Met-CH2 , Met-CH3 , and the systems of close by aromatic amino acid residues. Selected examples of proposed functions of 3-bridge clusters are discussed. Keywords and phrases: methionine; tyrosine; tryptophan; phenylalanine; non-covalent interactions; bioinform