NUCLEAR-MAGNETIC-RESONANCE STUDY AND SECONDARY STRUCTURE DETERMINATION OF THE ANTIBIOTIC PEPTIDE, AIBELLIN

Citation
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
Citations number
38
Categorie Soggetti
Biology,Agriculture,"Biothechnology & Applied Migrobiology","Food Science & Tenology
ISSN journal
09168451
Volume
58
Issue
12
Year of publication
1994
Pages
2188 - 2192
Database
ISI
SICI code
0916-8451(1994)58:12<2188:NSASSD>2.0.ZU;2-V
Abstract
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.