Thermodynamics of the interaction of insulin with its receptor.
Insulin binding to its cellular receptors is markedly dependent on the temperature. The thermodynamic parameters for the reaction of insulin with the high affinity state of its receptor have been evaluated with equilibrium studies at multiple temperatures between 5 degrees and 37 degrees C. The thermodynamics of the insulin-receptor interaction is not classical. The van't Hoff plot is not linear. Both the enthalpy and entropy changes, due to the formation of the hormone . receptor complex, decrease markedly with temperature, corresponding to a large heat capacity change of -766 cal/(mol deg) at 25 degrees C. The reaction is endothermic and entropically driven at low temperature and exothermic and enthalpically driven at higher temperature. This thermodynamic behavior is suggestive of a hydrophobic reaction and supports Blundell's concept that the loss of non-polar surface residues in the formation of the hormone . receptor complex is an important driving force of the reaction. Alternatively, this nonclassical behavior may indicate that the reaction of insulin with its receptor involves more than one step.
D002460:Cell Line; D006801:Humans; D007328:Insulin / Q000378:metabolism; D007700:Kinetics; D008214:Lymphocytes; D008433:Mathematics; D011485:Protein Binding; D011972:Receptor, Insulin / Q000378:metabolism; D013816:Thermodynamics
D007328:Insulin; D011972:Receptor, Insulin