Equilibrium unfolding of partially folded staphylococcal nuclease A2- and A3-forms is accompanied by the formation of an intermediate state.
Structural properties of an equilibrium intermediate formed upon urea-induced unfolding of more ordered staphylococcal nuclease A-forms (A2 and A3) are studied. The effect of association on the structural properties and conformational stability of this unfolding intermediate is also considered. A close structural similarity (including tendency for association) is shown between this intermediate and the least ordered A1-form, induced in the acid-unfolded nuclease by moderate sulfate or chloride concentrations.
Uversky
V N
VN
Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, 142292 Russia. uversky@vega.protres.ru
D008836:Micrococcal Nuclease / Q000737:chemistry*; D017510:Protein Folding
D008836:Micrococcal Nuclease