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A summary of the measured p<i>K</i> values of the ionizable groups in folded proteins
Protein Science · 2008 · Vol. 18(1) · pp. 247–251
Gerald R. Grimsley(Texas A&M University System)J. Martin Scholtz(Texas A&M University System)C. Nick Pace✉(Texas A&M University System)
Abstract
We tabulated 541 measured pK values reported in the literature for the Asp, Glu, His, Cys, Tyr, and Lys side chains, and the C and N termini of 78 folded proteins. The majority of these values are for the Asp, Glu, and His side chains. The average pK values are Asp 3.5 +/- 1.2 (139); Glu 4.2 +/- 0.9 (153); His 6.6 +/- 1.0 (131); Cys 6.8 +/- 2.7 (25); Tyr 10.3 +/- 1.2 (20); Lys 10.5 +/- 1.1 (35); C-terminus 3.3 +/- 0.8 (22) and N-terminus 7.7 +/- 0.5 (16). We compare these results with the measured pK values of these groups in alanine pentapeptides, and comment on our overall findings.
Protein Structure and DynamicsEnzyme Structure and FunctionMass Spectrometry Techniques and ApplicationsSide chainAlanineChemistryStereochemistryCrystallographyAmino acidBiochemistryOrganic chemistry
MeSH terms
Amino Acid SequenceAmino AcidsAspartic AcidHistidineHydrogen-Ion ConcentrationIsoelectric PointProteinsTitrimetryProtein Structure, TertiaryProtein FoldingGlutamic AcidNuclear Magnetic Resonance, Biomolecular
Funding
- National Institutes of Health
Citations
508
FWCI
5.93
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49
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97%
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References
What are the dielectric “constants” of proteins and how to validate electrostatic models?
Proteins Structure Function and Bioinformatics · 2001 · 940 citations
Very fast empirical prediction and rationalization of protein pK<sub>a</sub> values
Proteins Structure Function and Bioinformatics · 2005 · 2,031 citations
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