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Keywords:

  • β-Sheet;
  • protein stability;
  • protein design;
  • electrostatics;
  • side chain interactions

Abstract

We have evaluated the interaction energy of a three-residue ionic network constructed on the β-sheet surface of protein G using double mutant cycles. Although the two individual ion pairs were each stabilizing by ∼0.6 kcal/mol, the excess gain in stability for the triad was small (0.06 kcal/mol).