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1 H‐ and natural abundance 15 N‐nmr studies of a derivative of a rabies glycoprotein fragment
Author(s) -
Molinari Henriette,
Consonni Roberto,
Pegna Monica,
Zetta Lucia,
Neri Paolo,
Niccolai Neri,
Bonci Alessandra,
Lozzi Luisa,
Rustici Mauro,
Scarselli Maria
Publication year - 1991
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.360310616
Subject(s) - chemistry , fragment (logic) , derivative (finance) , glycoprotein , stereochemistry , p glycoprotein , biochemistry , algorithm , computer science , financial economics , economics , multiple drug resistance , antibiotics
Abstract Using a combination of one‐ and two‐dimensional methods, 1 H‐ and 15 N‐nmr spectroscopy has been employed to perform the complete assignment and the structural determination of the immunogenic undecapeptide CTTTNSRGTTT in DMSO solution. Nuclear Over‐hauser enhancement spectroscopy experiments indicated the presence of secondary structures, mainly turn‐like structures, which only represent a family, albeit a dominant one, of an ensemble of conformations available to the peptide. Since reverse turns may play an important role as intermediates in protein folding, the experimental observations described here may link the immunological and theoretical approaches to protein folding.