The thermal denaturation of bovine cardiac G-actin
- 1 April 1977
- journal article
- research article
- Published by Canadian Science Publishing in Canadian Journal of Biochemistry
- Vol. 55 (4) , 325-331
- https://doi.org/10.1139/o77-045
Abstract
The thermal denaturation of bovine cardiac G-actin was studied by UV difference spectroscopy and circular dichroism between pH 7.5-10.5. As with proteins previously studied, thermal unfolding is incomplete compared with unfolding by urea or guanidine hydrochloride. The same conformational change is observed over the pH range studied, and the available evidence indicates it is a 2-state transition. Thermodynamic analysis of the data shows that .DELTA.H0 and .DELTA.S0 [standard enthalpy and standard entropy] are strongly dependent on the temperature, that .DELTA.Cp (molar heat capacity) is 1300 cal deg-1 mol-1, and that G-actin has a temperature of maximum stability near -5.degree. C.This publication has 7 references indexed in Scilit:
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