S. Kumazawa et al., NUCLEAR-MAGNETIC-RESONANCE STUDY AND SECONDARY STRUCTURE DETERMINATION OF THE ANTIBIOTIC PEPTIDE, AIBELLIN, Bioscience, biotechnology, and biochemistry, 58(12), 1994, pp. 2188-2192
Aibellin is a 20-residue peptide antibiotic that has been isolated fro
m the fungus Verticimonosporium ellipticum. Sequence-specific assignme
nt of the H-1- and C-13-NMR signals of aibellin in a methanol solution
was achieved by using the two-dimensional NMR technique. Furthermore,
its secondary structure was characterized by circular dichroism (CD)
and NOESY spectra. The observed NOEs, (3)J(NHC alpha H) coupling const
ants and amide hydrogen-leuterium (H-D) exchange rates show that the p
eptide consisted of two alpha-helices and a bent structure around a Pr
o-14 residue.