Abstract
Microcalorimetric measurements of rat tail tendon collagen in different aqueous media show the following behavior of denaturation temperature (Td) and of denaturation enthalpy (deltaHd): H+ and OH- ions lower Td significantly beyond pH 4...11. Addition of salts (0.15 M) generally lowers Td in the range between pH 5 and 10, I- being more effective than Cl- at pH greater than i.p. However, in the region of pH less than i.p., I- raises Td to values above those of Cl- and even those of water. The value of deltaHd was found to be insensitive to pH over the pH range of 4...11. Hence the lowering of Td is assumed firstly to be due to a (ionic) disorganization of the water contacting the polypeptide chains and secondly to their mutual electrostatic repulsion. The appearance of deltaHd is thought mainly to be due to a rupture of interchain bonds.
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