A Conformational Transition in Concanavalin A. Conformational Differences between Intact and Fragmented Units

Abstract

Optical rotatory dispersion and circular dichroism studies reveal that between pH 5 and 7 concana-valin A undergoes a conformational transition which involves a slight loss of fJ-structure but no perturbation of aromatic residues. The dimer-tetramer association of concanavalin A may influence this transition but its contribution is relatively small and difficult to estimate. Near-u.v. circular di-chroism spectra reveal conformational differences between intact and fragmented units of the protein.