Question

In general, native proteins are in equilibrium with denatured forms: protein (native) ( ightleftharpoons) protein (denatured) For ribonuclease (a protein), the following concentration data for the two forms were experimentally determined for a total protein concentration of $1.0 imes 10^{-3}$ mol L$^{-1}$: egin{tabular}{|c|c|c|} hline Temperature ($^{circ}$C) & Native (mol L$^{-1}$) & Denatured (mol L$^{-1}$) \ hline 50 & $9.97 imes 10^{-4}$ & $2.57 imes 10^{-6}$ \ 100 & $8.6 imes 10^{-4}$ & $1.4 imes 10^{-4}$ \ hline end{tabular} Determine $Delta rH^{circ}$ of the denaturation reaction, assuming it to be independent of temperature.

          In general, native proteins are in equilibrium with denatured forms:
protein (native) (
ightleftharpoons) protein (denatured)
For ribonuclease (a protein), the following concentration data for the two forms were
experimentally determined for a total protein concentration of $1.0 	imes 10^{-3}$ mol L$^{-1}$:
egin{tabular}{|c|c|c|}
hline
Temperature ($^{circ}$C) & Native (mol L$^{-1}$) & Denatured (mol L$^{-1}$) \
hline
50 & $9.97 	imes 10^{-4}$ & $2.57 	imes 10^{-6}$ \
100 & $8.6 	imes 10^{-4}$ & $1.4 	imes 10^{-4}$ \
hline
end{tabular}
Determine $Delta rH^{circ}$ of the denaturation reaction, assuming it to be independent of temperature.

In general, native proteins are in equilibrium with denatured forms:
protein (native) (
ightleftharpoons) protein (denatured)
For ribonuclease (a protein), the following concentration data for the two forms were
experimentally determined for a total protein concentration of 1.0 imes 10^-3 mol L^-1:
egintabular|c|c|c|
hline
Temperature (^circC) Native (mol L^-1) Denatured (mol L^-1) hline
50 9.97 imes 10^-4 2.57 imes 10^-6 100 8.6 imes 10^-4 1.4 imes 10^-4 hline
endtabular
Determine Delta rH^circ of the denaturation reaction, assuming it to be independent of temperature.

Added by Xavier W.

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