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. Author manuscript; available in PMC: 2007 Feb 8.
Published in final edited form as: Biochemistry. 2007 Feb 6;46(5):1368–1379. doi: 10.1021/bi061949m

Figure 3. Selective deletion of the NH2-terminal variable region from TnT does not abolish binding to Tm.

Figure 3

Solid-phase protein binding curves of intact mouse cardiac TnT, McTnT-ND72 and McTnT-ND91 to Tm demonstrate the effect of TnT NH2-terminal truncations. The binding affinity of McTnT-ND72 to Tm was similar to that of the intact McTnT while the Tm binding affinity of McTnT-ND91 was decreased (P<0.001). There was no significant change in the maximal binding of McTnT-ND72 and McTnT-ND91 to Tm (inset). In contrast to the preserved activity of McTnT-ND72 with only the NH2-terminal variable region deleted, the decreased binding of McTnT-ND91 to Tm indicates that deletion into the conserved region damages the TnT core structure by disrupting the central Tm binding site (Fig. 1).