Examination of the conformational dynamics of photoregulated Concanavalin A by time-resolved light scattering

Abstract

Spiropyran-modified Concanavalin A (Con-A) displays photoregulated binding towards α-D-mannopyranoside, the photostimulated binding of the substrate originating from a structural perturbation of the protein upon photoisomerization of spiro-Con-A to the zwitterionic Con-A; time-resolved light scattering reveals that the structural change of the protein involves a shrinkage, and the dynamics of the protein shrinkage depend on the loading of Con-A with spiropyran units.