Inverse electrostatic effect: electrostatic repulsion in the unfolded state stabilizes a leucine zipper.

@article{Marti2004InverseEE,
  title={Inverse electrostatic effect: electrostatic repulsion in the unfolded state stabilizes a leucine zipper.},
  author={Daniel N Marti and Hans Rudolf Bosshard},
  journal={Biochemistry},
  year={2004},
  volume={43 39},
  pages={12436-47}
}
The pH-dependent stability of a protein is strongly affected by electrostatic interactions between ionizable residues in the folded as well as unfolded state. Here we characterize the individual contributions of charged Glu and His residues to stability and determine the NMR structure of the designed, heterodimeric leucine zipper AB consisting of an acidic A chain and a basic B chain. Thermodynamic parameters are compared with those of the homologous leucine zipper AB(SS) in which the A and B… CONTINUE READING