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

Stina Lindman1, Sara Linse, Frans A A Mulder

  • 1Department of Biophysical Chemistry, Lund University, Chemical Center, SE-22100 Lund, Sweden. stina.lindman@bpc.lu.se

Biochemistry
|November 23, 2006
PubMed
Summary

Protein charge interactions influence biological processes. Using carbon-13 NMR chemical shifts, researchers precisely measured protonation equilibria in a protein variant, revealing insights into local charge effects on protein electrostatics.

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