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. 2013 Mar 21;288(19):13431–13445. doi: 10.1074/jbc.M113.462861

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© 2013 by The American Society for Biochemistry and Molecular Biology, Inc.

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FIGURE 4. — L18-binding mutants uncouple initial recognition of the aggregate from its subsequent solubilization. A, binding of cpSRP43 to wild-type Lhcb₅ and L18 mutants H160C and H170C. The data were fit to Equation 1 (see “Experimental Procedures”) and gave K_d^app values of 10 nm for wild-type Lhcb₅ (black), 30 nm for Lhcb₅-H160C (blue), and 1.1 μm for Lhcb₅-L160C (red). B, concentration dependences for the equilibrium of disaggregation of LHCP by wild-type cpSRP43 (black) or mutant cpSRP43(R161A) (magenta). C and D, chaperone concentration dependences for the equilibrium (C) and kinetics (D) of disaggregation of Lhcb₅ (black), Lhcb₅-H160C (blue), and Lhcb₅-L170C (red) by wild-type cpSRP43.