Cα-Methyl, Cα-phenylglycine peptides: A structural study

SummaryIn 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 st...

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Bibliographic Details
Published inInternational journal of peptide research and therapeutics Vol. 5; no. 2-3; pp. 223 - 225
Main Authors Mossel, Eric, Formaggio, Fernando, Valle, Giovanni, Crisma, Marco, Toniolo, Claudio, Doi, Mitsunobu, Ishida, Toshimasa, Broxterman, Quirinus B., Kamphuis, Johan
Format Journal Article
LanguageEnglish
Published Leiden Springer Nature B.V 01.05.1998
Subjects
Amino acids
Conformation
Peptides
Phenylglycine
X-ray diffraction
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Summary:SummaryIn 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.
ISSN:0929-5666
1573-3149
1573-496X
1573-3904
DOI:10.1007/BF02443473