In a shorter Introduction we describe the usual experimental means of how t
o study protein stability and folding. Our work on stability of human stefi
ns A and B, determined by chemical, heat, and pH denaturation, is described
next. We explain the folding mechanism of human stefin B (as determined th
us far) and compare it to homologous human stefin A, in particular, the dep
endence of folding rates on the concentration of GuHCl. pH denaturation of
human stefin B (E.Zerovnik et al., Eur. J. Biochem. 1997, 245, 364-372) and
its folding to the native state are described in more detail.