Avadhesha Surolia
Articles written in Journal of Biosciences
Volume 9 Issue 3-4 December 1985 pp 203-212
Prediction and comparison of the secondary structure of legume lectins
M Joginadha Swamy M Venkata Krishna Sastry Avadhesha Surolia
Secondary structure prediction for the 4 legume lectins: Concanavalin A, soybean agglutinin, favabean lectin and lentil lectin, was done by the method of Chou and Fasman. This prediction shows that these four lectins fall into a structurally distinct class of proteins, containing high amounts of β-sheet and β-turns. There is a notable similarity in the gross structure of these proteins; all four of them contain about 40–50% of β-sheet, 35–45 % β-turn and 0–10% of α-helix. When the secondary structure of corresponding residues in each pair of these lectins was compared, there was a striking similarity in the Concanavalin A-soybean agglutinin and favabean lectin-lentil lectin pairs, and considerably less similarity in the other pairs, suggesting that these legume lectins have probably evolved in a divergent manner from a common ancestor. A comparison of the predicted potential β-turn sites also supports the hypothesis of divergent evolution in this class of lectins.
Volume 31 Issue 5 December 2006 pp 551-556
Dynamic light scattering study of peanut agglutinin: Size, shape and urea denaturation
Sagarika Dev Avadhesha Surolia
Peanut agglutinin (PNA) is a homotetrameric protein with a unique open quaternary structure. PNA shows non-two state profile in chaotrope induced denaturation. It passes through a monomeric molten globule like state before complete denaturation (Reddy
Volume 48, 2023
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