Fig. 2: Monomer-dimer equilibrium in FOR005 and GL. | Nature Communications

Fig. 2: Monomer-dimer equilibrium in FOR005 and GL.

From: Mechanistic insights into the aggregation pathway of the patient-derived immunoglobulin light chain variable domain protein FOR005

Fig. 2

A Concentration-dependent 1H,15N HSQC spectra for the patient protein FOR005. Protein concentrations of 14/18 μM (black), 170 μM (red), 650 μM (orange) and 1.1 mM (green) have been employed. Residues that show large concentration dependent chemical changes are highlighted with a dashed blue circle. In the inset, the spectral region containing G101 is shown enlarged for FOR005 and GL. B 1H,15N chemical shift difference Δδ for spectra recorded at the highest and lowest concentration for FOR005 (red) and GL (green) as a function of residue. C Protein concentration dependent chemical shift difference Δδ for FOR005 (left) and GL (right). To fit the dissociation constant Kd, the chemical shifts of the residues K38, A42, F99 and G101 were employed. The non-linear fit of the dilution data yields (1.74 ± 0.61) mM and (3.60 ± 0.32) mM for FOR005 and GL, respectively. Structural models of the canonical (D) and alternate (E) dimer interfaces. The crystal structure of FOR005 VL (PDB 5L6Q) was employed to represent the canonical dimer interface. To obtain the alternate dimer structure a homology model has been generated using the X-ray structure of AL09 H87Y (PDB: 2KQN). Source data are provided as a Source Data file.

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