title: Histidine in continuum electrostatics protonation state calculations.
abstract: A modification to the standard continuum electrostatics approach to calculate protein pK(a)s, which allows for the decoupling of histidine tautomers within a two-state model, is presented. Histidine with four intrinsically coupled protonation states cannot be easily incorporated into a two-state formalism, because the interaction between the two protonatable sites of the imidazole ring is not purely electrostatic. The presented treatment, based on a single approximation of the interrelation between histidine's charge states, allows for a natural separation of the two protonatable sites associated with the imidazole ring as well as the inclusion of all protonation states within the calculation.
authors.affiliation: Department of Chemistry, University of California, Davis, California 95616, USA.
authors.forename: Vernon
authors.initials: V
authors.lastname: Couch
authors.forename: Alexei
authors.initials: A
authors.lastname: Stuchebrukhov
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism; D003198:Computer Simulation; D006639:Histidine / Q000737:chemistry* / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007093:Imidazoles / Q000737:chemistry; D008836:Micrococcal Nuclease / Q000737:chemistry* / Q000378:metabolism*; D008956:Models, Chemical; D008958:Models, Molecular; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D011522:Protons; D055672:Static Electricity; D013482:Superoxide Dismutase / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D007093:Imidazoles; D011522:Protons; D006639:Histidine; C029899:imidazole; D013482:Superoxide Dismutase; D008836:Micrococcal Nuclease
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