Journal
JOURNAL OF CHEMICAL THEORY AND COMPUTATION
Volume 6, Issue 10, Pages 3259-3266Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ct1003093
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Funding
- Conselho Nacional de Desenvolvimento Cientifico e Tecnologico (CNPq)
- Fundacao de Amparo a Pesquisa do Estado de Sao Paulo (FAPESP)
- Swedish Research Council
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Proton exchange between titratable amino acid residues and the surrounding solution gives rise to exciting electric processes in proteins. We present a proton titration scheme for studying acid-base equilibria in Metropolis Monte Carlo simulations where salt is treated at the Debye-Huckel level. The method, rooted in the Kirkwood model of impenetrable spheres, is applied on the three milk proteins alpha-lactalbumin, beta-lactoglobulin, and lactoferrin, for which we investigate the net-charge, molecular dipole moment, and charge capacitance. Over a wide range of pH and salt conditions, excellent agreement is found with more elaborate simulations where salt is explicitly included. The implicit salt scheme is orders of magnitude faster than the explicit analog and allows for transparent interpretation of physical mechanisms. It is shown how the method can be expanded to multiscale modeling of aqueous salt solutions of many biomolecules with nonstatic charge distributions. Important examples are protein-protein aggregation, protein-polyelectrolyte complexation, and protein-membrane association.
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