Báo cáo Y học: Equilibrium unfolding and conformational plasticity of troponin I and T
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The structures and stabilities of recombinant chickenmuscletroponin I (TnI) and T (TnT) were investigated by a com-bination of bis-ANS binding and equilibrium unfoldingstudies.Unlike most folded proteins, isolated TnI and TnTbind the hydrophobic fluorescent probe bis-ANS, indicatingthe existence of solvent-exposed hydrophobic domains intheir structures.Bis-ANS 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, whichcan be explained by burial of previously exposed hydro-phobicdomainsuponassociationof the subunits to formthenative troponin complex....
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Báo cáo Y học: Equilibrium unfolding and conformational plasticity of troponin I and T
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Báo cáo Y học: Equilibrium unfolding and conformational plasticity of troponin I and T
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