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The effect of homologous amino acid replacement on the conformation of oligopeptides. II. Synthesis of co‐oligopeptides containing methionine and glycine
Author(s) -
Champi Jim,
Steinfeld Alvin S.,
Naider Fred,
Becker Jeffrey M.
Publication year - 1978
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.1978.360170913
Subject(s) - chemistry , oligopeptide , hexafluoroacetone , glycine , residue (chemistry) , homologous series , stereochemistry , methionine , serine , amino acid , polymer chemistry , crystallography , organic chemistry , peptide , biochemistry , enzyme
The synthess of 18 co‐oligopeptides of L ‐methionine and glycine is reported. A series of oligomers, Boc‐Gly‐Met n ‐OMe ( n = 1–6), and six hexamers‐containing five methionyl and one glycyl residue were synthesized using the mixed anhydride procedure. Polarimetric studies give evidence that oligomers in the Boc‐Gly‐Met n ‐Ome series are essentially disordered in hexafluoroacetone sesquihydrate but begin forming secondry structures at n > 4 in trifluorethanol. Difference in the molar rotation values found for the six hexamers in hexafluoroacetone sesquihydrate may indicate that these compounds, while primirily disordered, are present in slightly different conformations.