Solution conformation of the C-terminal domain of skeletal troponin C.

Proton magnetic resonance spectroscopy has been used to study the cation(Mg2+ , Ca2+)-dependent conformational states of the C-terminal domain of rabbit skeletal troponin C under a variety of solution conditions. Nuclear Overhauser data and paramagnetic probe observations provide definition of the configuration of this region of troponin C. Comparative study of homologous proteins identify common features of the tertiary structure relevant to the biding reaction. Complex formation with troponin I and the drug intercative conformational response to cation coordination and the binding of the drug and troponin I are discussed. [ABSTRACT FROM AUTHOR]