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Empirical relationships between protein structure and carboxyl pKa values in proteins by William R. Forsyth; Jan M. Antosiewicz; Andrew D. Robertson is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is Empirical relationships between protein structure and carboxyl pKa values in proteins about?

Relationships between protein structure and ionization of carboxyl groups were investigated in 24 proteins of known structure and for which 115 aspartate and 97 glutamate pK(a) values are known. Mean pK(a) values for aspartates and glutamates are < or = 3.4 (+/-1.0) and 4.1 (+/-0.8), respectively. For aspartates, mean pK(a) values are 3.9 (+/-1.0) and 3.1 (+/-0.9) in acidic (pI 8) proteins, respectively, while mean pK(a) values for glutamates are approximately 4.2 for acidic and basic proteins. Burial of carboxyl groups leads to dispersion in pK(a) values: pK(a) values for solvent-exposed groups show narrow distributions while values for buried groups range from 5.5 and most are found in active sites or ligand-binding sites. These carboxyl groups are buried and usually accept no more than one hydrogen bond. Aspartates and glutamates at the N-termini of helices have mean pK(a) values of 2.8 (+/-0.5) and 3.4 (+/-0.6), respectively, about 0.6 units less than the overall mean values.

Who reads Empirical relationships between protein structure and carboxyl pKa values in proteins?

Author

William R. Forsyth; Jan M. Antosiewicz; Andrew D. Robertson

Publisher

John Wiley and Sons; Wiley (John Wiley & Sons); Wiley-Liss Inc; Wiley (ISSN 0887-3585)

Published

2002

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)