Rogers NK, 1989

Rogers presents a complete set of pK values in his chapter entitled "The role of electrostatic interactions in the structure of globular proteins" in the book Prediction of protein structure and the principles of protein conformation edited by Fasman (1). Both the presentation and data are modeled after an earlier chapter by Timasheff, and these values are identical to the pK values given by Timasheff (2). These pK values are "quoted for the idealized side chains" and may vary in folded proteins. Rogers also notes, parenthetically, that the pK values vary "between sources in the literature."

Amino acid pK values from Rogers NK, 1989 (1).

Group

3.7

†‡

ASP

4.4

†¶

GLU

4.4

†§

HIS

7.05

†€

8.0

†¥

CYS

9.5

†

TYR

10.0

†*

LYS

10.0

†•

ARG

†£

† Data from Figure 2.

‡ The reported range of pK values is 3.6–3.8. The value recorded here is the mean value of this range.

¶ The reported range of pK values is 4.0–4.8. The value recorded here is the mean value of this range.

§ The reported range of pK values is 4.0–4.8. The value recorded here is the mean value of this range.

€ The reported range of pK values is 6.3–7.8. The value recorded here is the mean value of this range.

¥ The reported range of pK values is 7.5–8.5. The value recorded here is the mean value of this range.

* The reported range of pK values is 9.5–10.5. The value recorded here is the mean value of this range.

• The reported range of pK values is 9.6–10.4. The value recorded here is the mean value of this range.

£ The pK value is reported as >13.

(1) Rogers NK (1989) The role of electrostatic interactions in the structure of globular proteins in Prediction of protein structure and the principles of protein conformation (Fasman G, Ed.), Plenum Press, New York.