pH-Dependent pKa Values in Proteins—A Theoretical Analysis of Protonation Energies with Practical Consequences for Enzymatic Reactions
Author:
Affiliation:
1. Structural Biology/Bioinformatics, University of Bayreuth, Universitätsstrasse 30, BGI, 95447 Bayreuth, Germany
Publisher
American Chemical Society (ACS)
Subject
Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/jp908926w
Reference26 articles.
1. Electrostatic calculations of side-chain pKa values in myoglobin and comparison with NMR data for histidines
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3. Nuclear Magnetic Resonance Studies of Protonation of Some Polyaminocarboxylate Compounds Containing Asymmetric Carbon Atoms.
4. Determination of the p K a of the four Zn 2+ -coordinating residues of the distal finger motif of the HIV-1 nucleocapsid protein: Consequences on the binding of Zn 2+ 1 1Edited by M. F. Summers
5. A Novel View of pH Titration in Biomolecules
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