The creatine kinase isozyme MB from myocardium is a heterodimer. The structure and conformational flexibility of CK-MB can be compared with CK-MM and CK-BB, the parent homodimers, to determine those changes in shape and dynamics necessary for heterodimerization.
The search for stable folding intermediates in the assembly of monomeric arginine kinase and dimeric creatine kinase continues, adding on to the discovery of a compact, native like structure in both these phosphagen kinases. Efforts are continuing to determine structural features on the folding pathway of arginine kinase, using site-specific mutagenesis .
Work is also underway to evaluate the dynamics of the molten globule state of alpha lactalbumin using time resolved fluorescence methods.
The cockroach is a rich sourceof arginine kinase, an enzyme essential for mobility. Several approaches are being studied to characterize the structure, kinetics and inhibition of this enzyme including identification of new strongly inhibitory transition state analogs.