Figure 3
From: Conformational folding and disulfide bonding drive distinct stages of protein structure formation
The formation of the intra-subunit disulfide bond licenses the subsequent core rearrangement. (A) Secretory CRP mutants with N-terminal signal peptide of CRP or ALP (Alkaline phosphatase) were expressed by COS-7 (left) or E. coli cells (right). Mutating cysteines or a.a. 166–178 helix prevented the secretion of native CRP. (B) The configuration of strands in addition to C to H before Cys36-Cys97 bonding was examined with appropriate CRP mutants (Table S2). Beside strand I, other strands were found to be either misassembled or unfolded. (C) A schematic diagram summarizes the core configuration before and after formation of the intra-subunit disulfide bond. Data were presented as mean +/− S.E. Each data point represents the mean of data obtained from at least 3 independent experiments.
