Fig. 3: Antibody variable domain CDR loop and framework region charge.
From: Reliable repurposing of the antibody interactome inside the cell
a The majority of variable heavy domain CDR loops are negatively charged and normally distributed around −1.81 to −1.69 dependent on maturation state. VH framework regions are predominantly positively charged and distributed around +2.77 to +3.10. This effect is observed irrespective of variable domain numbering scheme (Supplementary Table 2). Conversely, light chain CDR and framework charge display overlapping distributions. A slight skew to positive and negative respectively is conserved between Chothia and Kabat but not IMGT numbering schemes (Supplementary Table 2). b Salt-bridge bonding between β-strands D and F of the 3B5H10 antibody variable domains. Bonding distances annotated. c Charge substitution mutation VL Arg61Glu reduces 3B5H10-derived scFv intrabody solubility by breaking the salt-bridge in b. Error bars represent one standard deviation, n = 7 and 5 biological replicates, P = 0.058 (two-tailed, two-sample equal variance t test). Source data are provided as a Source Data file.
