Authors: T Dergez F Könczöl N Farkas J Belőgyi D Lõrinczy
Publish Date: 2005/05/01
Volume: 80, Issue: 2, Pages: 445-449
Abstract
The heat capacity of contractile proteins actin and myosin was studied in psoas muscle of rabbit in strongly and weakly binding state of myosin to actin as a function of temperature by DSC Deconvolution of the unfolding scans makes possible to characterize the structural domains of the macromolecules We tried to approach the unfolding process in different intermediate state of ATP hydrolysis The thermal transitions were calorimetrically irreversible therefore the twostate irreversible model that describes fairly well the denaturation of different proteins was used for evaluation of the denaturation processes in muscle fibers in strongly rigor ADP and weakly binding states ATPmiddotVi ADPmiddotAlF4 of myosin to actin Deconvolution resulted in four transitions the first three transition temperatures were almost independent of the intermediate states of muscle the last transition temperature was shifted to higher temperature when the buffer solution was manipulated The mean values in strongly binding states were Tm1=529plusmn07degC Tm2=579plusmn07degC Tm3=637plusmn10degC and Tm4=678plusmn07degC but the last transition increased to higher temperature depending on the Pi analogue
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