STABILITY AND FOLDING STUDIES OF TWO HOMOLOGOUS PROTEINS, HUMAN STEFINS A AND B.
Eva Žerovnik1, Roman Jerala2 , Louise Kroon-Žitko1 and Vito Turk1
1 Department of Biochemistry and Molecular Biology, Jožef Stefan Institute, Jamova 39, 1000 Ljubljana, Slovenia 2 Laboratory for Molecular Modeling and NMR Spectroscopy, National Institute of Chemistry, Hajdrihova 19, 1000 Ljubljana, Slovenia
In a shorter Introduction we describe the usual experimental means of how to study protein stability and folding. Our work on stability of human stefins A and B, determined by chemical, heat and pH denaturation, is described next. We explain the folding mechanism of human stefin B (as determined thus far) and compare it to homologous human stefin A, in particular, the dependence of folding rates on the concentration of GuHCl. pH denaturation of human stefin B ( E.Žerovnik et al., Eur. J. Biochem. 1997, 245, 364-372 ) and its folding to the native state are described in more detail.