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Preferred Spatial Arrangement of the Aromatic Side Chains in Linear Oligopeptides Containing Tyrosine
Author(s) -
Wüthrich Kurt,
De Marco Antonio
Publication year - 1976
Publication title -
helvetica chimica acta
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.74
H-Index - 82
eISSN - 1522-2675
pISSN - 0018-019X
DOI - 10.1002/hlca.19760590637
Subject(s) - chemistry , side chain , tyrosine , residue (chemistry) , oligopeptide , stereochemistry , vicinal , aromatic amino acids , amino acid residue , amino acid , peptide , peptide sequence , biochemistry , organic chemistry , gene , polymer
1 H‐NMR. studies of the protected linear tetrapeptides CF 3 CO‐Gly‐Gly‐ L ‐Tyr‐ L ‐Ala‐OCH 3 , CF 3 CO‐Gly‐ L ‐Ala‐ L ‐Tyr‐ L ‐Ala‐OCH 3 and CF 3 CO‐Gly‐ L ‐Ala‐ L ‐Tyr‐Gly‐OCH 3 showed that the side chain of the tyrosyl residue was in all three peptides preferentially oriented towards the amino terminus of the peptide chain. This preferred spatial arrangement of the aromatic side chain was manifested in the chemical shifts of the amino acid residue preceding tyrosine and in the vicinal spin‐spin coupling constants 3 J HCαCβH of tyrosine.