Temperature dependence denaturational heat capacity

Fig. 4. Temperature dependence of the specific enthalpy of denaturation of myoglobin and ribonuclease A (per mole of amino acid residues) in solutions with pH and buffer providing maximal stability of these proteins and compensation of heat effects of ionization (see Privalov and Khechinashvili, 1974). The broken extension of the solid lines represents a region that is less certain due to uncertainty in the A°CP function (see Fig. 2). The dot-and-dash lines represent the functions calculated with the assumption that the denaturation heat capacity increment is temperature independent.

The Calorimetrically Obtained van t Hoff Enthalpy In a manner analogous to that used to obtain the van t Hoff enthalpy from the fractional change in the optical absorbance, one can use the temperature dependence of the fractional enthalpy as a function of temperature to determine an effective enthalpy. We will adopt the notation to represent the total enthalpy associated with the denaturation transition. It can be obtained from an integration of the excess heat capacity, corrected for the baselines, as discussed before ... 

The general thermodynamic properties of proteins reported above give rise to several questions What do the asymptotic (at Tx) values of the denaturation enthalpy and entropy mean and why are they apparently universal for very different proteins Why should the denaturation enthalpy and entropy depend so much on temperature and consequently have negative values at low temperature In other words, why is the denaturation increment of the protein heat capacity so large, with a value such that the specific enthalpies and entropies of various proteins converge to the same values at high temperature ... 

Figure 2.13. Dependence of partial molar heat capacity of a protein on the temperature (thermogram). The denatured protein always has a higher heat capacity than the native one. The high heat capacity at the peak stems from the increasing fluctuation in the system. In contrast to the native state, many more conformations are possible and the protein switches back and forth between different...

The simplest way to derive thermodynamic parameters from UV melting data is to apply a van t Hoff analysis of the data by assuming a two-state model (i.e. native and denatured states) and that the difference in heat capacities of the native and denatured states, ACp°, is zero (13-16) (more complex models are described in Section 5). At each temperature the absorbance can be used to calculate the fraction of strands in the native and denatured states, thereby allowing the calculation of an equilibrium constant (10). Thus, the absorbance versus temperature profile is used to determine the temperature dependence of... 

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