ISSN:
1573-3904
Keywords:
β-bend
;
disubstituted glycines
;
fully extended conformation
;
310-helix
;
Cα-methylated α-amino acids
Source:
Springer Online Journal Archives 1860-2000
Topics:
Chemistry and Pharmacology
Notes:
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.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1023/A:1008809532026
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