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Protein Ionizable Groups: pK Values and Their Contribution to Protein Stability and Solubility
Open accessAbstract
The structure, stability, solubility, and function of proteins depend on their net charge and on the ionization state of the individual residues. Consequently, biochemists are interested in the pK values of the ionizable groups in proteins and how these pK values depend on their environment. We review what has been learned about pK values of ionizable groups in proteins from experimental studies and discuss the important contributions they make to protein stability and solubility.
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Cited by
Graphical analysis of pH-dependent properties of proteins predicted using PROPKA
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Proteome-pI: proteome isoelectric point database
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Metadata
- Authors
- Pace, C. N., Grimsley, G. R., & Scholtz, J. M.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2009-05
- Volume
- 284
- Issue
- 20
- Pages
- 13285-13289
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2070144513
- Cited by
- 461
- References
- 37
- FWCI
- 7.56
- Type
- journal article
- Language
- en
- Open access
- hybrid
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- creativecommons.org/licenses/by/4.0/ (vor, 4253 d)
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- Pace, C. N., Grimsley, G. R., & Scholtz, J. M. (2009). Protein Ionizable Groups: pK Values and Their Contribution to Protein Stability and Solubility. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.r800080200
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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