The structures and stabilities of recombinant chickenmuscle troponin I (TnI) and T (TnT) were investigated by a com-bination of bis-ANS binding and equilibrium unfolding most folded proteins, isolated TnI and TnT bind the hydrophobic fluorescent probe bis-ANS, indicating the existence of solvent-exposed hydrophobic domains in their binding to binary or ternary mix-tures of TnI, TnT and troponin C (TnC) in solution is sig-nificantly lower than binding to the isolated subunits, which can be explained by burial of previously exposed hydro-phobicdomainsuponassociationof the subunits to formthe native troponin complex
