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Mono and two‐dimensional 500‐MHz characterization of synthetic bombesin and related peptides in DMSO and DMSO–water ,
Author(s) -
Di Bello Carlo,
Gozzini Luigia,
Tonellato Mauro,
Corradini Maria Grazia,
D'Auria Gabriella,
Paolillo Livio,
Trivellone Enrico
Publication year - 1989
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.360280139
Subject(s) - chemistry , dimethyl sulfoxide , peptide , coupling constant , bombesin , proton nmr , proton , characterization (materials science) , protein secondary structure , two dimensional nuclear magnetic resonance spectroscopy , nuclear overhauser effect , crystallography , stereochemistry , nuclear magnetic resonance spectroscopy , organic chemistry , nanotechnology , biochemistry , physics , receptor , materials science , particle physics , quantum mechanics , neuropeptide
The proton nmr characterization of bombesin (BBS) and of two peptide fragments corresponding to the (1–6) and (6–14) sequences has been carried out at 500 MHz in dimethyl sulfoxide (DMSO‐d 6 ) using two‐dimensional (2D) homo and 1 H‐ 13 C heterocorrelated techniques. All resonances in the nmr spectra have been assigned and several coupling constants have been measured. The backbone J αCHNH coupling constants are quite similar and around 7.8–8.2 Hz, pointing to an unfolded structure in DMSO‐d 6 . The possibility of secondary structures in highly viscous mixtures of DMSO‐d 6 –water was investigated. The existence of sequential nuclear Overhauser enhancement (NOE) effects in the C‐terminal nonapeptide section may indicate a preferential site for secondary structuring.