pH-dependent processes in proteins.
Recent improvements in the understanding of electrostatic interactions in proteins serve as a focus for the general topic of pH-dependent processes in proteins. The general importance of pH-dependent processes is first set out in terms of hydrogen ion equilibria, stability, ligand interactions, assembly, dynamics, and events in related molecular systems. The development of various theoretical treatments includes various formalisms in addition to the solvent interface model developed by Shire et al. as an extension of the Tanford-Kirkwood treatment. A number of detailed applications of the model are presented and future potentialities are sketched.
D000818:Animals; D001665:Binding Sites; D004355:Drug Stability; D006454:Hemoglobins / Q000378:metabolism; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D046911:Macromolecular Substances; D008722:Methods; D008954:Models, Biological; D008958:Models, Molecular; D009211:Myoglobin / Q000378:metabolism; D011485:Protein Binding; D011487:Protein Conformation; D011506:Proteins / Q000378:metabolism*; D013816:Thermodynamics
D006454:Hemoglobins; D046911:Macromolecular Substances; D009211:Myoglobin; D011506:Proteins