Conformational change in the C-terminal domain is responsible for the initiation of creatine kinase thermal aggregation.

ABSTRACT: Protein conformational changes may be associated with particular properties such as its function, transportation, assembly, tendency to aggregate, and potential cytotoxicity. In this research, the conformational change that is responsible for the fast destabilization and aggregation of rabbit muscle creatine kinase (EC 2.7.3.2) induced by heat was studied by intrinsic fluorescence and infrared spectroscopy. A pretransitional change of the tryptophan microenvironments was found from the intrinsic fluorescence spectra. A further analysis of the infrared spectra using quantitative second-derivative and two-dimensional correlation analysis indicated that the changes of the beta-sheet structures in the C-terminal domain and the loops occurred before the formation of intermolecular cross-beta-sh

SUBMITTER: He HW 

PROVIDER: S-EPMC1366765 | biostudies-literature | 2005 Oct

REPOSITORIES: biostudies-literature