Characterization of the Partially Folded Monomeric Intermediate of Creatine Kinase

IntroductionRecent studies of the protein folding pathway andintermediate states in vitro and in vivo haveinduced much interest in the importance ofunderstanding the propertiesof partially structuredintermediates[1 7] . Studies have suggested thatintermed…

Characterization of the Partially Folded Monomeric Intermediate of Creatine Kinase

The importance of understanding the protein folding pathway and intermediates is well recognized on the basis of extensive studies of protein folding in vitro and in vivo. Creatine kinase (CK) is a typical model for studying unfolding and refolding of proteins due to several interesting properties. Recent studies on the folding of CK show that its partially folded monomeric intermediate is present kinetically and is stable at equilibrium. The present paper contains 33 references as a mini review to characterize the properties of CK from studies on the CK folding pathway. Characterization of these intermediates is an essential step toward understanding the mechanism of protein folding. Some well determined schemes are suggested as protein folding models.