Abstract
In order to obtain further information on the role played by phenyl ring position in the Cα-methylated α-amino acid side chain on peptide preferred conformation, the crystal-state structural preferences of Cα-methyl, Cα-phenylglycine peptides have been determined by X-ray diffraction. This study shows that either the fully extended conformation or the β-bend/310-helical structures are adopted by peptides characterized by this Cα-methylated, β-branched, aromatic α-amino acid.
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