Electrostatic contributions to residue-specific protonation equilibria and proton binding capacitance for a small protein.

@article{Lindman2006ElectrostaticCT,
  title={Electrostatic contributions to residue-specific protonation equilibria and proton binding capacitance for a small protein.},
  author={Stina Lindman and Sara Linse and Frans A. A. Mulder and Ingemar Andr{\'e}},
  journal={Biochemistry},
  year={2006},
  volume={45 47},
  pages={13993-4002}
}
Charge-charge interactions in proteins are important in a host of biological processes. Here we use 13C NMR chemical shift data for individual aspartate and glutamate side chain carboxylate groups to accurately detect site-specific protonation equilibria in a variant of the B1 domain of protein G (PGB1-QDD). Carbon chemical shifts are dominated by changes in the electron distribution within the side chain and therefore excellent reporters of the charge state of individual groups, and the data… CONTINUE READING