Tryptophan Anisotropy Decay of Liver Alcohol Dehydrogenase

Intrinsic Tryptophan Anisotropy Decay of Liver Alcohol Dehydrogenase 

Liver alcohol dehydrogenase (LADH) is a dimer with two tryptophan residues in each identical subunit and a total molecular weight of 80 hDa. One of the residues is exposed to the solvent (tip- IS), and one residue is buried (tip-314). This buried residue can be selectively excited on the red edge of the absorption spectrum at 300 nm.  

The anisotropy decay of LADH excited at 300 nm is shown in Ft gure 11.13. The decay was found to be a single exponential with a correlation time of 33 ns. This single correlation time can be compared with that predicted for a hydrated sphere (0.2 g of H20/g of protein) from Eq. [10.52]), which is 31 ns at 20 C. Hence, this tryptophan residue appears to be rigidly held within the protein matrix. 

---

A. Intrinsic Tryptophan Anisotropy Decay of Liver Alcohol Dehydrogenase... 

---