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Critical chain length for helix formation in L ‐methionine oligopeptides
Author(s) -
Becker Jeffrey M.,
Naider Fred
Publication year - 1974
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.1974.360130907
Subject(s) - random hexamer , chemistry , oligopeptide , trimer , methionine , circular dichroism , stereochemistry , helix (gastropod) , crystallography , amino acid , biochemistry , organic chemistry , peptide , dimer , ecology , snail , biology
The circular dichroism of a series of L ‐methionine oligopeptides [BOC‐(Met) n ‐OMe] was examined in trifluoroethanol and hexafluoroacetone sesquihydrate. The results indicate that the trimer through the hexamer exists predominantly in disordered conformations in these solvents. An abrupt change in the CD pattern at the heptamer in trifluoroethanol suggests that L ‐methionine oligopeptides begin forming helices at this chain length.