Enthalpy, entropy and heat capacity changes induced by binding of calcium ions to cardiac troponin C.
Microcalorimetric titrations have been used to study the binding of Ca2+ to cardiac troponin C. Measurements were made both in the presence and in the absence of Mg2+, and at temperatures of 5 degrees, 15 degrees and 25 degrees C. Changes in enthalpy, entropy and heat capacity of troponin C associated with Ca binding have been determined. Cardiac troponin C exhibited a decrease in enthalpy and an increase in entropy associated with Ca binding. Enthalpy changes increased linearly with temperature, indicating that the Ca binding causes negative changes in the heat capacity of troponin C. These results show that the Ca binding causes a strong hydrophobic effect and a tightening of the molecular structure of cardiac troponin C.
D000818:Animals; D002118:Calcium / Q000378:metabolism*; D002151:Calorimetry; D002417:Cattle; D007700:Kinetics; D009124:Muscle Proteins / Q000378:metabolism*; D009206:Myocardium / Q000378:metabolism*; D013816:Thermodynamics; D014336:Troponin / Q000378:metabolism*; D019209:Troponin C
D009124:Muscle Proteins; D014336:Troponin; D019209:Troponin C; D002118:Calcium