Nuclear Magnetic Resonance Study and Secondary Structure Determination of the Antibiotic Peptide, Aibellin
| Autor: | Tetsuo Hayase, Mina Kanda, Hideyuki Aoyama, Shigenori Kumazawa, Masami Utagawa, Hiroyuki Ohtani, Takashi Mikawa, Isao Chiga, Tsuneo Hino |
|---|---|
| Rok vydání: | 1994 |
| Předmět: |
Circular dichroism
Magnetic Resonance Spectroscopy Stereochemistry Molecular Sequence Data Peptide Applied Microbiology and Biotechnology Biochemistry Protein Structure Secondary Analytical Chemistry chemistry.chemical_compound Residue (chemistry) Nuclear magnetic resonance Amide Amino Acid Sequence Molecular Biology Protein secondary structure chemistry.chemical_classification Organic Chemistry General Medicine Verticimonosporium ellipticum Anti-Bacterial Agents chemistry Methanol Peptides Two-dimensional nuclear magnetic resonance spectroscopy Antimicrobial Cationic Peptides Biotechnology |
| Zdroj: | Bioscience, Biotechnology, and Biochemistry. 58:2188-2192 |
| ISSN: | 1347-6947 0916-8451 |
| DOI: | 10.1271/bbb.58.2188 |
| Popis: | Aibellin is a 20-residue peptide antibiotic that has been isolated from the fungus Verticimonosporium ellipticum. Sequence-specific assignment of the 1H- and 13C-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, 3JNHC alpha H coupling constants and amide hydrogen-deuterium (H-D) exchange rates show that the peptide consisted of two alpha-helices and a bent structure around a Pro-14 residue. |
| Databáze: | OpenAIRE |
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