Conformation of .beta.-methylmelibiose bound to the ricin B-chain as determined from transferred nuclear Overhauser effects
- 1 October 1992
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 31 (39) , 9339-9349
- https://doi.org/10.1021/bi00154a003
Abstract
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 almost-equal-to 170-degrees) and minor (omega almost-equal-to -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.This publication has 16 references indexed in Scilit:
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