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pK values of the ionizable groups of proteins
Journal article   Open access   Peer reviewed

pK values of the ionizable groups of proteins

Richard L. Thurlkill, Gerald R. Grimsley, J. Martin Scholtz and C. Nick Pace
Protein science, Vol.15(5), pp.1214-1218
05/01/2006
DOI: 10.1110/ps.051840806
PMCID: PMC2242523
PMID: 16597822
url
https://europepmc.org/articles/pmc2242523View
Published (Version of record) Open Access

Abstract

We have used potentiometric titrations to measure the pK values of the ionizable groups of proteins in alanine pentapeptides with appropriately blocked termini. These pentapeptides provide an improved model for the pK values of the ionizable groups in proteins. Our pK values determined in 0.1 M KCl at 25°C are: 3.67±0.03 (α-carboxyl), 3.67±0.04 (Asp), 4.25±0.05 (Glu), 6.54±0.04 (His), 8.00±0.03 (α-amino), 8.55±0.03 (Cys), 9.84±0.11 (Tyr), and 10.40±0.08 (Lys). The pK values of some groups differ from the Nozaki and Tanford (N&T) pK values often used in the literature: Asp (3.67 this work vs. 4.0 N&T); His (6.54 this work vs. 6.3 N&T); α-amino (8.00 this work vs. 7.5 N&T); Cys (8.55 this work vs. 9.5 N&T); and Tyr (9.84 this work vs. 9.6 N&T). Our pK values will be useful to those who study pK perturbations in folded and unfolded proteins, and to those who use theory to gain a better understanding of the factors that determine the pK values of the ionizable groups of proteins.
For the Record peptide model compounds pH titration pK values protein ionizable groups

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