Conformation of .beta.-methylmelibiose bound to the ricin B-chain as determined from transferred nuclear Overhauser effects
| Autor: | V. L. Bevilacqua, J. H. Prestegard, Yangmee Kim |
|---|---|
| Rok vydání: | 1992 |
| Předmět: |
Models
Molecular chemistry.chemical_classification Magnetic Resonance Spectroscopy Ricinus Stereochemistry Molecular Conformation Disaccharide Glycosidic bond Ricin Nuclear Overhauser effect Ligands Biochemistry Omega Plants Toxic chemistry.chemical_compound chemistry Covalent bond Plant Lectins Melibiose Conformational isomerism |
| Zdroj: | Biochemistry. 31:9339-9349 |
| ISSN: | 1520-4995 0006-2960 |
| DOI: | 10.1021/bi00154a003 |
| Popis: | Transferred nuclear Overhauser effect (TRNOE) experiments have revealed a change in the torsion angles about the alpha-1-6 glycosidic bond of methyl beta-melibioside upon binding of the melibioside to the ricin B-chain (Rb). A full relaxation rate matrix simulation of experimental buildup curves aided in quantitative interpretation of 1D selective inversion recovery TRNOE experiments. The data are consistent with a model in which both major (omega approximately 170 degrees) and minor (omega approximately -60 degrees) conformers for methyl beta-melibioside are significantly populated in solution while the Rb/methyl beta-melibioside complex has little of the minor conformer populated. The results indicate that the ricin B-chain excludes binding of certain ligand conformations on the basis of unfavorable interactions between the protein surface and remote portions of the disaccharide system. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|