Heat capacity, changes during protein

An additional feature of this technique is that it is very easy to obtain the heat capacity change during binding, Cp = dH/dT, by simply measuring the enthalpy at different temperatures. Studies with model proteins have shown that the change in heat capacity is negative (ACp = —0.32 cal mol/deg-A ) when... 

Water at apolar surfaces has rather distinctive thermodynamic properties, in particular an unusually low entropy and high heat capacity. Displacement of water from apolar surfaces to bulk during protein folding and ligand binding dominates observed heat-capacity changes of the whole system. Consequently, apolar surface hydration has received much more attention than that of polar surfaces. Water... 

Having considered those intermolecular interactions that contribute to overall net measured thermodynamic parameters, we turn now to a review of thermodynamic measurements of protein-carbohydrate binding reported during the last five years. Values reported prior to this time can be found in earlier reviews. Calorimetrically derived changes in enthalpies, entropies, free energies and molar heat capacity that occur during protein-carbohydrate binding are shown in Table 8. 

The must is subsequently sterilized, boiling being the most commonly used method (McConnell and Schramm, 1995 Navratil et al., 2001 Ukpabi, 2006). Heat treatments also have the potential to alter the antioxidant capacity by changing their phenolic profiles (Wintersteen et al., 2005). However, other techniques are described in the literature. These include the use of metabisulfite (sodium or potassium salts or in commercial form as Campden tablets)—releases sulfur dioxide that either kills or inactivates most microbes (McConnell and Schramm, 1995 Roldan et al., 2011), sulfur dioxide gas (Pereira et al., 2009 Ukpabi, 2006), pasteurization (McConnell and Schramm, 1995 Mendes-Ferreira et al., 2010), and ultrafiltration, with a 50-kDa molecular weight cutoff (McConnell and Schramm, 1995). Some of these methods also promote the removal of proteins by denaturation and coagulation, resulting in more rapid clarification during maturation. 

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