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Mobility of oligopeptides on normal‐phase silica: Effect of positional isomerism
Author(s) -
Naider Fred,
Huchital Michael,
Becker Jeffrey M.
Publication year - 1983
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.360220511
Subject(s) - oligopeptide , chemistry , residue (chemistry) , peptide , stereochemistry , hexa , amino acid residue , cyclic peptide , crystallography , organic chemistry , peptide sequence , biochemistry , gene
Isomeric oligopeptides composed of five methionyl residues and one glycyl residue or of five γ‐methyl‐ L ‐glutamyl residues and one glycyl residue all exhibit marked differences in retention on normal‐phase silica. When the glycyl residue is at internal positions of hexa or heptapeptides, the peptide elutes most rapidly form the μPorasil column. Comparison of the effect of positional isomerism on retention in short oligopeptides with the effect on retention of hexamers and heptamers suggests that a change in peptide conformation may be responsible for the change in oligopeptide mobility.