Contributions of a highly conserved VH/VL hydrogen bonding interaction to scFv folding stability and refolding efficiency.

@article{Tan1998ContributionsOA,
  title={Contributions of a highly conserved VH/VL hydrogen bonding interaction to scFv folding stability and refolding efficiency.},
  author={Phuay Heng Tan and Brenda M Sandmaier and Patrick S. Stayton},
  journal={Biophysical journal},
  year={1998},
  volume={75 3},
  pages={1473-82}
}
The assembly of single-chain Fv (scFv) antibody fragments, consisting of an interconnected variable heavy chain (VH) and variable light chain (VL), is a cooperative process that requires coupled folding and domain association. We report here an initial investigation of VH/VL domain-domain assembly with a site-directed mutagenesis study that probes a highly conserved VH/VL hydrogen bonding interaction. Gln168 of the S5 scFv (Kabat VH 39) is absolutely conserved in 95% of all VH, and Gln44 (Kabat… CONTINUE READING