@article{uoadl:3054483,
    volume = "8",
    number = "2",
    pages = "77-87",
    journal = "Letters in Peptide Science",
    issn = "0929-5666",
    keywords = "conformation analysis; LHRH agonist; molecular modeling; nuclear
magnetic resonance spectroscopy",
    BIBTEX_ENTRY = "article",
    year = "2001",
    author = "Benaki, DC and Paxinou, E and Magafa, V and Pairas, GN and and Manessi-Zoupa, E and Cordopatis, PA and Mikros, E",
    abstract = "The nonapeptide Leuprorelin, one of the LHRH agonists, was studied by
means of 2D nuclear magnetic resonance spectroscopy and molecular
modeling. NOESY spectra in aqueous/deuterated methanol solution (50%
H2O/CD3OD) at low temperature (268 K) revealed short-range nOe
connectivities (i, i+1), characteristic of flexibility of the molecule.
The H-N-H-N sequential connectivities observed provide evidence that the
sequence has the propensity to form a bend involving residues 5 and 6
and the N-terminal segment. The alpha-proton chemical shifts compared to
random coil and additional data from the amide proton temperature
coefficients support this assumption. One long-range nOe cross peak
between H-2(alpha)-H-NEth is indicative of proximity between C- and
N-termini.",
    title = "Conformational analysis of the nonapeptide leuprorelin using NMR and
molecular modeling",
    doi = "10.1023/A:1015036903464"
}