Abstract
1-Anilino-8-naphthalene sulfonic acid (ANS), a hydrophobic dye, is widely used to monitor conformational changes occuring in proteins during their folding/unfolfing. Using cardiotoxin III (whose conformation remains unperturbed even in 6 M urea) from the Taiwan Cobra ( Naja naja atra) venom, it is demonstrated that chaotropic denaturant such as urea directly competes with the interaction between ANS and the protein. The results presented in this report, in our opinion, has significant implication(s) in the area of protein folding, arising out of ANS binding experiments.
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Schedule a callMore From: Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular Enzymology
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