Two-Dimensional 1H-NMR and CD Structural Analysis in a Micellar Medium of a Bovine alphas1-Casein Fragment having Benzodiazepine-Like Properties
| Autor: | Michel Marraud, Marc Lecouvey, Piotr Orlewski, Régis Vanderesse, Céline Frochot, Jean-Luc Gaillard, Manh Thong Cung, Alain Driou, Laurent Miclo, Guy Linden |
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| Rok vydání: | 1997 |
| Předmět: |
Models
Molecular Circular dichroism Magnetic Resonance Spectroscopy Protein Conformation Stereochemistry Biochemistry Micelle Protein Structure Secondary Benzodiazepines Protein structure Amphiphile Animals Dimethyl Sulfoxide Micelles Chemistry Hydrogen bond Circular Dichroism Caseins Sodium Dodecyl Sulfate Water Hydrogen Bonding Aromaticity Nuclear magnetic resonance spectroscopy Peptide Fragments Crystallography Proton NMR Tyrosine Cattle |
| Zdroj: | European Journal of Biochemistry. 248:872-878 |
| ISSN: | 1432-1033 0014-2956 |
| DOI: | 10.1111/j.1432-1033.1997.00872.x |
| Popis: | The conformation of the benzodiazepine-like decapeptide, YLGYLEQLLR, corresponding to residues 91-100 of bovine alphaS1-casein, has been examined in SDS micelles using CD, two-dimensional 1H-NMR and restrained molecular-dynamics simulation. Evidence is presented that the decapeptide adopts a rigid structure in water/SDS micellar medium, but not in water or dimethylsulfoxide. The three-dimensional structure, consistent with the proton-proton distances obtained from the quantitative analysis of the two-dimensional NOEs, was generated by restrained energy minimization and molecular-dynamics simulation. In water/SDS micellar medium, YLGYLEQLLR adopts an amphipathic helicoid structure with distinct hydrophobic and hydrophilic faces. The relative disposition of the tyrosine aromatic rings was compared with that of the aromatic rings in the benzodiazepines. |
| Databáze: | OpenAIRE |
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