Journal ArticleOpen Access
<scp>L</scp>-Methionyl-<scp>L</scp>-tyrosine monohydrate
Author Affiliations
Hampton University, Louisiana State University, Southern University and Agricultural and Mechanical College, Southern University
Published InIUCrData
Year2023
Citations2
Abstract
The study of the oxidation of various proteins necessitates scrutiny of the amino acid sequence. Since methionine (Met) and tyrosine (Tyr) are easily oxidized, peptides that contain these amino acids are frequently studied using a variety of oxidation methods, including, but not limited to, pulse radiolysis, electrochemical oxidation, and laser flash photolysis. To date, the oxidation of the Met–Tyr dipeptide is not fully understood. Several investigators have proposed a mechanism of intramolecular electron transfer between the sulfide radical of Met and the Tyr residue. Our elucidation of the structure and absolute configuration of L-Met–L-Tyr monohydrate, C 14 H 20 N 2 O 4 S·H 2 O (systematic name: (2 S )-2-{[(2 S )-2-amino-4-methylsulfanylbutanoyl]amino}-3-(4-hydroxyphenyl)propanoic acid monohydrate) is presented herein and provides…
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