STEPWISE HEAT DENATURATION OF MYOSIN HELICAL FRAGMENTS

  • 1 January 1979
    • journal article
    • research article
    • Vol. 24  (1) , 46-50
Abstract
Scanning microcalorimetry was used to study heat denaturation of [rabbit] myosin tail helical fragments, light meromyosin and the LF-3 subfragment. The data obtained were explained by the existence of a set of quasi-independent, cooperative regions. Probable location sites of separate cooperative regions in the helical part of the molecule were indicated. Sites of cooperative breaks are in agreement with sites of predominant cleavage of the myosin tail by proteolytic enzymes. The total denaturation enthalpy for each of the helical fragments per H bond at 100.degree. C is slightly less (5.4 .+-. 0.8 kJ.cntdot.mol-1) than the corresponding value for globular proteins.

This publication has 1 reference indexed in Scilit: