Figure 8
From: Disulfide driven folding for a conditionally disordered protein
hCox17 oxidative folding followed by real-time solution NMR. Reduced hCox17 was allowed to refold and HSQCs were collected along the reaction. Residues were assigned and their intensities measured. (A) Normalized chemical shift intensities depicted according to the color bar, where in white is 0% formation and in red 100% formation. Residues 1 to 25 remained disordered and are not taken into account, His 47 was not assigned. (B) Normalized chemical shift intensities after 22 h of reaction shown on top of hCox17 solution NMR structure (PDB file: 2RN9), color code as in A. Folding kinetics from Cys 26, Cys 36, Cys 45 and Cys 55 amino acids are represented as an example. In the x axis time is represented as hours, and in y axis normalized chemical shift intensities.
