Structure of the cyclohexapeptide cleromyrine II trihydrate
| Autor: | Jean-Paul Declercq, Bernard Tinant, S. Bashwira, Claude Hootele |
|---|---|
| Rok vydání: | 1990 |
| Předmět: |
chemistry.chemical_classification
Magnetic Resonance Spectroscopy Molecular Structure Hydrogen bond Stereochemistry Molecular Sequence Data General Medicine Crystal structure Plants Antiparallel (biochemistry) Peptides Cyclic General Biochemistry Genetics and Molecular Biology Cyclic peptide Mass Spectrometry chemistry X-Ray Diffraction Intramolecular force X-ray crystallography Molecule Amino Acid Sequence Hydrate Crystallization |
| Zdroj: | Acta crystallographica. Section C, Crystal structure communications. 46 |
| ISSN: | 0108-2701 |
| Popis: | C29H40N6O7.3H2O, Mr = 638.7, trigonal, P3(1)21, a = 14.190 (2), c = 29.833 (4) A, V = 5202 (1) A3, Z = 6, Dx = 1.22 g cm-3, Cu K alpha, lambda = 1.54178 A, mu = 7.8 cm-1, F(000) = 2052, T = 291 K, R = 0.069 for 1942 observed reflections. The new cyclohexapeptide cleromyrine II was isolated from Clerodendrum myricoides. Its structure was established by spectroscopic and X-ray diffraction methods as cyclo(-Gly-Tyr-Gly-Pro-Leu-Pro-). The conformation essentially consists of two beta-turns including the Pro residues and one central very short antiparallel beta-sheet stabilized by two intramolecular hydrogen bonds: N(Tyr2)...O(Leu5) = 2.94 (2) A and N(Leu5)...O(Tyr2) = 3.02 (2) A. |
| Databáze: | OpenAIRE |
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