Effect of chaotropic denaturant on the binding of 1-anilino-8-naphthalene sulfonic acid to proteins.
1-Anilino-8-naphthalene sulfonic acid (ANS), a hydrophobic dye, is widely used to monitor conformational changes occurring in proteins during their folding/unfolding. 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.
Kumar
T K
TK
Department of Chemistry, National Tsing Hua University, Hsinchu, Taiwan, ROC.
Jayaraman
G
G
Lin
W Y
WY
Yu
C
C
D000817:Anilino Naphthalenesulfonates; D000818:Animals; D002942:Circular Dichroism; D004179:Cobra Cardiotoxin Proteins / Q000737:chemistry*; D004546:Elapid Venoms / Q000737:chemistry*; D017815:Elapidae; D005456:Fluorescent Dyes; D009682:Magnetic Resonance Spectroscopy; D011485:Protein Binding; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*
D000817:Anilino Naphthalenesulfonates; D004179:Cobra Cardiotoxin Proteins; D004546:Elapid Venoms; D005456:Fluorescent Dyes; D011506:Proteins; C082202:cardiotoxin III, Naja naja atra; C027132:1-anilino-8-naphthalenesulfonate