The backbone and side chain conformations of the cyclic tetrapeptide HC-toxin
| Autor: | William A. Gibbons, Lynda M. Ciuffetti, Mark R. Pope, Paolo Mascagni, Herman W. Knoche |
|---|---|
| Rok vydání: | 1983 |
| Předmět: |
Magnetic Resonance Spectroscopy
Chloroform Tetrapeptide Protein Conformation Stereochemistry Biophysics Cell Biology Nuclear magnetic resonance spectroscopy Nuclear Overhauser effect Peptides Cyclic Biochemistry Nmr data chemistry.chemical_compound chemistry Side chain Molecular Biology Mathematics Toxins Biological |
| Zdroj: | Biochemical and Biophysical Research Communications. 113:10-17 |
| ISSN: | 0006-291X |
| DOI: | 10.1016/0006-291x(83)90424-2 |
| Popis: | A study of the conformational parameters of HC-toxin and its diacetyl derivative in chloroform solution has been carried out. Two-dimensional NMR spectroscopy and the nuclear Overhauser effect have been used in order to determine connectivities (assignments and sequence) and approximate torsion angles and interproton distances. The results are consistent with a bis-γ-turn conformation previously reported for dihydrochlamydocin. Model building based upon NMR data supports a D configuration for Ala 2 and Pro 4 residues. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|