Residue-specific pKa determination of lysine and arginine side chains by indirect 15N and 13C NMR spectroscopy: application to apo calmodulin.

@article{Andr2007ResiduespecificPD,
  title={Residue-specific pKa determination of lysine and arginine side chains by indirect 15N and 13C NMR spectroscopy: application to apo calmodulin.},
  author={Ingemar Andr{\'e} and Sara Linse and Frans A. A. Mulder},
  journal={Journal of the American Chemical Society},
  year={2007},
  volume={129 51},
  pages={15805-13}
}
Electrostatic interactions in proteins can be probed experimentally through determination of residue-specific acidity constants. We describe here triple-resonance NMR techniques for direct determination of lysine and arginine side-chain protonation states in proteins. The experiments are based on detection of nonexchangeable protons over the full range of pH and temperature and therefore are well suited for pKa determination of individual amino acid side chains. The experiments follow the side… CONTINUE READING
25 Citations
0 References
Similar Papers

Citations

Publications citing this paper.
Showing 1-10 of 25 extracted citations

Similar Papers

Loading similar papers…