Protein denaturation processes under stress conditions such as pH, den
aturant and heat are evaluated by employing several approaches such as
aqueous two-phase partitioning and circular dichroism (CD) measuremen
t in order to determine the conformational states and surface properti
es of proteins, It Is suggested that the manner of conformational chan
ge of protein from the native state to the molten globule one does not
depend on these sorts of stresses if both the strength of stress and
surface properties of proteins are normalized between the above two st
ates. By using these normalization parameters, eight proteins used in
this study mere simply divided into two groups namely monomeric protei
ns and oligomeric one. On the other hand, the strength of stress which
inducing protein denaturation up to the molten globule state greatly
depends on the sort of stresses or protein species. From these conside
rations, the possibility of using effective stress-mediated separation
process of protein is suggested as an application of the analysis of
the stress responsive behaviors of proteins.