In order to obtain further information on the role played by phenyl ring position in the C-alpha-methylated alpha-amino acid side chain on peptide preferred conformation, the crystal-state structural preferences of C-alpha-methyl, C-alpha-phenylglycine peptides have been determined by X-ray diffraction. This study shows that either the fully extended conformation or the beta-bend/3(10)-helical structures are adopted by peptides characterized by this C-alpha-methylated, beta-branched, aromatic alpha-amino acid.
C-alpha-methyl, C-alpha-phenylglycine peptides: A structural study
FORMAGGIO, FERNANDO;TONIOLO, CLAUDIO;
1998
Abstract
In order to obtain further information on the role played by phenyl ring position in the C-alpha-methylated alpha-amino acid side chain on peptide preferred conformation, the crystal-state structural preferences of C-alpha-methyl, C-alpha-phenylglycine peptides have been determined by X-ray diffraction. This study shows that either the fully extended conformation or the beta-bend/3(10)-helical structures are adopted by peptides characterized by this C-alpha-methylated, beta-branched, aromatic alpha-amino acid.File in questo prodotto:
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