The DOI matches its Crossref record; 30 of the 30 references it cites were found in a registry or an index.
Arginine: Its p Ka value revisited
Open accessAbstract
Using complementary approaches of potentiometry and NMR spectroscopy, we have determined that the equilibrium acid dissociation constant (p Ka value) of the arginine guanidinium group is 13.8 ± 0.1. This is substantially higher than that of ∼12 often used in structure‐based electrostatics calculations and cited in biochemistry textbooks. The revised intrinsic p Ka value helps explains why arginine side chains in proteins are always predominantly charged, even at pH values as great as 10. The high p Ka value also reinforces the observation that arginine side chains are invariably protonated under physiological conditions of near neutral pH. This occurs even when the guanidinium moiety is buried in a hydrophobic micro‐environment, such as that inside a protein or a lipid membrane, thought to be incompatible with the presence of a charged group.
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Cites
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Dissociation Constants of Organic Bases in Aqueous Solution
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A summary of the measured p K values of the ionizable groups in folded proteins
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Large shifts in pK a values of lysine residues buried inside a protein
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Chemical mechanisms of histone lysine and arginine modifications
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Cited by
Martin, E. W., & Holehouse, A. S. (2020) · Emerging Topics in Life Sciences · doi:10.1042/etls20190164 · Cited by 281
Metadata
- Authors
- Fitch, C. A., Platzer, G., Okon, M., Garcia‐Moreno E., B., & McIntosh, L. P.
- Venue
- Protein Science
- Publisher
- Wiley
- Published
- 2015-03-22
- Volume
- 24
- Issue
- 5
- Pages
- 752-761
- ISSN
- 0961-8368 (ISSN-L)
- 1469-896X
- OpenAlex
- W1489827117
- Cited by
- 383
- References
- 30
- FWCI
- 8.49
- Type
- journal article
- Language
- en
- Open access
- bronze
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