title: On the origin of the electrostatic barrier for proton transport in aquaporin.
abstract: The nature of the electrostatic barrier for proton transport in aquaporins is analyzed by semimacroscopic and microscopic models. It is found that the barrier is associated with the loss of the generalized solvation energy upon moving from the bulk solvent to the center of the channel. It is clarified that our solvation concept includes the effect of the protein polar groups and ionized residues. The nature of the contributions to the solvation barrier is examined by using the linear response approximation. It is found that the residues in the NPA region contribute much less than what would be deduced from calculations that do not consider the protein reorganization. It is clarified that the contributions of different structural or electrostatic elements to the solvation barrier can be established by removing these elements and examining the corresponding effect on the barrier height. Using this definition and "mutating" the NPA residues to their non-polar analogues establishes that these residues do not provide the major contribution to the solvation barrier.
authors.affiliation: Department of Chemistry, University of Southern California, 3620 McClintock Ave. SGM 418, Los Angeles, CA 90089-1062, USA.
authors.forename: Anton
authors.initials: A
authors.lastname: Burykin
authors.forename: Arieh
authors.initials: A
authors.lastname: Warshel
mesh_terms: D051398:Aquaporin 1; D020346:Aquaporins / Q000737:chemistry* / Q000502:physiology*; D001671:Biochemistry / Q000379:methods; D003198:Computer Simulation; D007700:Kinetics; D008958:Models, Molecular; D015233:Models, Statistical; D008962:Models, Theoretical; D009154:Mutation; D011485:Protein Binding; D011487:Protein Conformation; D011522:Protons; D055672:Static Electricity; D013816:Thermodynamics; D014867:Water / Q000737:chemistry
chemical_list: D020346:Aquaporins; D011522:Protons; D014867:Water; D051398:Aquaporin 1