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Opioid peptides in micellar systems: Conformational analysis by CD and by one-dimensional and two-dimensional 1H-nmr spectroscopy

✍ Scribed by Lucia Zetta; Roberto Consonni; Antonio De Marco; Renato Longhi; Ernesto Manera; Giuseppe Vecchio

Publisher
Wiley (John Wiley & Sons)
Year
1990
Tongue
English
Weight
772 KB
Volume
30
Category
Article
ISSN
0006-3525

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✦ Synopsis

SYNOPSIS

0-Endorphin has been studied in SDS micelles by one-and two-dimensional nmr spectroscopy ( 1D and 2D nmr) , and to explore the influence of peptide length and composition on the polypeptide structure, the investigation was extended to a number of fragments.

The nmr results are compared with those obtained from CD experiments and discussed. in terms of a secondary structure that involves the central region of @-endorphin.

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