Formation of electrostatic interactions on the protein-folding pathway.

@article{Oliveberg1996FormationOE,
  title={Formation of electrostatic interactions on the protein-folding pathway.},
  author={Mikael Oliveberg and A. R. Fersht},
  journal={Biochemistry},
  year={1996},
  volume={35 8},
  pages={2726-37}
}
We describe a novel method of obtaining information about the structures of transient conformations on the folding pathway from their ionization equilibria: the H+ -titration behavior of a protein residue is determined in detail by its environment. We follow the consolidation of electrostatic interactions in the folding process by comparing the acid-titration behavior of four conformations on the folding pathway of barnase: the denatured state (D); the folding intermediate (I); the major… CONTINUE READING