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. Author manuscript; available in PMC: 2009 Jan 1.
Published in final edited form as: Cell Biochem Biophys. 2007 Nov 28;50(1):1–22. doi: 10.1007/s12013-007-9005-0

Table 2.

A summary of formulas for the apparent linearity in the denaturation free energy curves (mapp) and the corresponding preferential binding parameter differences (ΔΓ23) for different models of protein denaturation. See text for an explanation of the symbols. We have used the fact that m3 = ρ31 for the Local-bulk model (140) and (ρ3ρ1)P,T=V1V3 for the Exchange 2 model. N33’ is the derivative of N33 with respect to cosolvent concentration

Model mapp ΔΓ23
m-value m mρ3a33
Transfer a33ρ3iniαiΓi3 iniαiΓi3
Binding site ΔnKb1+Kbρ3 ΔnKbρ31+Kbρ31a33
Exchange 1 Δn(Ke1)a33ρ1+ρ3+ρ3(Ke1) Δnρ3(Ke1)ρ1+ρ3+ρ3(Ke1)
Exchange 2 meρ1ϕ1 meρ3ρ1ϕ1a33
Local-bulk (KP1)b1OΔASAa33m1ϕ1(1+KPS3m3m1) ρ3(KP1)b1OΔASAm1ϕ1(1+KPS3m3m1)
LCPE A[1+B(N33+ρ3N33)] ρ3A[1+B(N33+ρ3N33)]a33