Properties of troponin C acetylated at lysine residues

Acetylation of lysine residues in rabbit skeletal troponin C (TnC) causes drastic decrease in the overall stability of the protein. The positively charged lysine side chains located in the N-terminal domain moderate TnC's structural stability and interactions with Ca2+ and other troponin components. The lower stability of the acetylated form is due to the intramolecular repulsive forces caused by the increase in the overall negative charge of the molecule.