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concluded that a potent inhibitor of protein phosphatase 1, DARPP-32 (dopamine- and CAMP-regulated phosphoprotein with an apparent molecular mass, of 32,000 on SDS- polyacrylamide gel electrophoresis), although this protein is characterized by mostly random coil conformation, has a max of 352 nm, low fluorescence anisotropy values indicative of the independent segmental motions of the peptide chain surrounding fluorophore, and is characterized by accessibility to quencher comparable to that of proteins containing exposed fluorophores, it can be further unfolded by 8 M urea, as evidenced by further decrease of fluorescence anisotropy (Neyroz et al., 1993)