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pK values of the ionizable groups of proteins.
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pH-dependent random coil (1)H, (13)C, and (15)N chemical shifts of the ionizable amino acids: a guide for protein pK a measurements.
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A statistical approach to the prediction of pK(a) values in proteins.
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Hydrogen bonding markedly reduces the pK of buried carboxyl groups in proteins.
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[3] Inferences drawn from physicochemical studies of crystallogenesis and precrystalline state.
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Asp79 makes a large, unfavorable contribution to the stability of RNase Sa.
J Mol Biol. 2005 Dec 9;354(4):967-78. doi: 10.1016/j.jmb.2005.09.091. Epub 2005 Oct 21.
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Measuring pK(a) values in protein folding transition state ensembles by NMR spectroscopy.
J Am Chem Soc. 2005 Jun 29;127(25):8904-5. doi: 10.1021/ja051942c.
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Charge-charge interactions in the denatured state influence the folding kinetics of ribonuclease Sa.
Protein Sci. 2005 Jul;14(7):1934-8. doi: 10.1110/ps.051401905. Epub 2005 Jun 3.
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Determinants of cysteine pKa values in creatine kinase and alpha1-antitrypsin.
Proteins. 2004 Dec 1;57(4):799-803. doi: 10.1002/prot.20261.
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Prediction of pKa and redox properties in the thioredoxin superfamily.
Protein Sci. 2004 Oct;13(10):2744-52. doi: 10.1110/ps.04804504. Epub 2004 Aug 31.

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