Functional characterization of the human α-cardiac actin mutations Y166C and M305L involved in hypertrophic cardiomyopathy
DNase I, a specific actin binding protein, forms a stable complex with actin. CD spectroscopy was used to study the question whether the structure of actin and DNase I in their complex are identical with those of the individual components. Far and near UV analysis was used to study the secondary structure and the environment of aromatic chromophores. CD spectroscopic results on actin, DNase I and on their complex in solution are presented which show that no structural change takes place as a result of actin-DNase I complex formation and indicate the absence of aromatic chromophores on the interface of the actin and DNase I in their complex. CD spectroscopy proved to be a convenient technique for studying the interactions between actin and actin binding proteins in solution.