Disrupting the hydrophobic patches at the antibody variable/constant domain interface: improved in vivo folding and physical characterization of an engineered scFv fragment.

@article{Nieba1997DisruptingTH,
  title={Disrupting the hydrophobic patches at the antibody variable/constant domain interface: improved in vivo folding and physical characterization of an engineered scFv fragment.},
  author={Lars Nieba and Annemarie Honegger and Claus M. Krebber and Andreas Pl{\"u}ckthun},
  journal={Protein engineering},
  year={1997},
  volume={10 4},
  pages={
          435-44
        }
}
By constructing Fv and single-chain Fv (scFv) fragments of antibodies, the variable domains are taken out of their natural context in the Fab fragment, where they are associated with the constant domains of the light (CL) and heavy chain (CH1). As a consequence, all residues of the former variable/constant domain interface become solvent exposed. In an analysis of 30 non-redundant Fab structures it was found that at the former variable/constant domain interface of the Fv fragment the frequency… CONTINUE READING

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