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. Author manuscript; available in PMC: 2011 Dec 7.
Published in final edited form as: Biochemistry. 2010 Nov 12;49(48):10339–10348. doi: 10.1021/bi101428e

Figure 9.

Figure 9

Calculated NMR chemical shifts for the protons in the Tyr16-phenolate hydrogen bond (red), the Asp103-phenolate hydrogen bond (blue), and the Tyr16-Tyr57 hydrogen bond (green) as functions of the solution pKa of the substituted phenolate. These chemical shifts were determined from QM/MM calculations of the phenolate bound to pKSI D40N with (A) the unmodified hydrogen-bonding network, (B) the Y32F mutation, and (C) the Y32F/Y57F mutations. All calculations included Tyr16, Asp103, Asp40Asn, residue 32, residue 57, and the phenolate in the QM region.