Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 2009 Jan;18(1):247-51.
doi: 10.1002/pro.19.

A summary of the measured pK values of the ionizable groups in folded proteins

Affiliations

A summary of the measured pK values of the ionizable groups in folded proteins

Gerald R Grimsley et al. Protein Sci. 2009 Jan.

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.

PubMed Disclaimer

Figures

Figure 1
Figure 1
Distribution of the measured pK values for Asp (A), Glu (B), and His (C). The arrow on the top axis of each figure indicates the intrinsic pK value as measured in alanine pentapeptides.

References

    1. Thurlkill RL, Grimsley GR, Scholtz JM, Pace CN. pK values of the ionizable groups of proteins. Protein Sci. 2006;15:1214–1218. - PMC - PubMed
    1. Nozaki Y, Tanford C. Examination of titration behavior. Methods Enzymol. 1967;11:715–734.
    1. Tollinger M, Crowhurst KA, Kay LE, Forman-Kay JD. Site-specific contributions to the pH dependence of protein stability. Proc Natl Acad Sci USA. 2003;100:4545–4550. - PMC - PubMed
    1. Cho JH, Raleigh DP. Mutational analysis demonstrates that specific electrostatic interactions can play a key role in the denatured state ensemble of proteins. J Mol Biol. 2005;353:174–185. - PubMed
    1. Marti DN. Apparent pKa shifts of titratable residues at high denaturant concentration and the impact on protein stability. Biophys Chem. 2005;118:88–92. - PubMed

Publication types

LinkOut - more resources