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Location of a binding site for 1-anilinonaphthalene-8-sulfonate on calmodulin
Archives of Biochemistry and Biophysics
|January 1, 1984
Abstract:
The quenching by radiationless energy transfer of the ultraviolet fluorescence of Tyr-99 and Tyr-138 by bound 1-anilinonaphthalene-8-sulfonate (1,8-ANS) has been employed to determine the separation of a hydrophobic binding site of 1,8-ANS from each of the tyrosines. The results suggest that the dominant binding site is located in the N-terminal region of domain III.