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Fluorescence Anisotropy as a Tool to Study Protein-protein Interactions
Published on: October 21, 2016
Circular dichroism and fluorescence investigations on Vicia faba lectin-saccharide binding
The Biochemical Journal
|April 1, 1988
Abstract:
Vicia faba lectin contained 40-57% beta-conformation, 4-23% alpha-conformation along with random coil at pH 7.2 depending upon the analytical methods used. The percentage of beta-conformation increased with the addition of N-acetyl-D-glucosamine or methyl alpha-D-mannopyranoside. The structural transitions of V. faba lectin were affected by alkali at pH 9.6 and 10.6. Binding constants and free energy changes for the interaction between V. faba lectin and N-acetyl-D-glucosamine and methyl alpha-D-mannopyranoside were estimated at pH 7.2 using the c.d. and fluorescence methods.

