Identification of Regions Involved in Substrate Binding and Dimer Stabilization within the Central Domains of Yeast Hsp40 Sis1
Figure 6
Fluorescence studies of Sis1 and Sis1_Δ124–174.
The lone tryptophan residue in Sis1 and Sis1_Δ124–174 (5 µM protein concentration) was used as a probe to investigate changes in the local protein structure and in hydrodynamic parameters, such as rotational diffusion, caused by the deletion of 50 amino acids in Sis1. The (A) fluorescence emission spectra, (B) tryptophan anisotropy and (C) tryptophan quenching results are shown. All experiments were performed in triplicate.