The Electrostatic Interaction of Rigid, Globular Proteins with Arbitrary Charge Distributions

McClurg, Richard B.; Zukoski, Charles F.

doi:10.1006/jcis.1998.5858

Cited by 36 publications

(50 citation statements)

References 41 publications

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“…Although like-charged, significant protein attraction may arise from higher order moments [23,24]. Further, electric multipolar moments due to acidic and basic side chains have been shown to correlate with the tertiary structure of globular proteins [25] and nonspherical models for electrophoretic mobility also incorporate higher order moments as a descriptor for electrostatic anisotropy [26].…”

Section: Charge Anisotropy Via Electric Multipolesmentioning

confidence: 97%

Anisotropic protein–protein interactions due to ion binding

Lund

2016

Colloids and Surfaces B: Biointerfaces

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Section: Charge Anisotropy Via Electric Multipolesmentioning

confidence: 97%

Anisotropic protein–protein interactions due to ion binding

Lund

2016

Colloids and Surfaces B: Biointerfaces

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“…A variety of different methods are available to calculate the electrostatic free energy between protein molecules (Phillies, 1974;Gilson et al, 1988;Coen et al, 1995;Coen et al, 1996;McClurg and Zukoski, 1998;Sader and Lenhoff, 1998;Asthagiri et al, 1999;Farnum and Zukoski, 1999;Neal et al, 1999;Grant, 2001;Bratko et al, 2002). Typically, these methods rely on a dielectric continuum representation for the solvent (Friedman, 1985).…”

Section: Introductionmentioning

confidence: 99%

Electrostatic Interactions between Peptides and the Molecular Chaperone DnaK

et al. 2003

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“…McClurg and Zukoski [19] used the linearized Poisson-Boltzmann equation to estimate the electrostatic interaction energy for two charged dipolar proteins. They provided analytical expressions for the multipolar-expansion solution for the protein-protein interaction potential as a function of protein-protein orientation.…”

Section: Introductionmentioning

confidence: 99%

Forces between aqueous nonuniformly charged colloids from molecular simulation

Striolo

Bratko

et al. 2002

The Journal of Chemical Physics

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NVT Monte Carlo simulation results are presented for the forces between charged colloids within the primitive model for electrolytes. The calculations show that when charged colloids have a net dipole moment, a strong attraction can arise at short separations. The attractive force is not purely electrostatic; significant contributions follow from hard-sphere collisions between the electrolyte ions and the colloidal particles. In divalent electrolyte solutions, non-uniformly charged colloids show an oscillatory force profile as a function of separation, due to layering of electrolyte ions around the interacting colloids.Simulation results are compared to two analytical models derived from classical Debye-Hückel screened potentials. In the first model, contributions from charge-charge, dipole-dipole, and charge-dipole interactions are independently angle-averaged and then added to obtain the colloid-colloid potential. In the second model, the pair potential is obtained by simultaneously angle-averaging all interactions.Our results show that simultaneous angle-averaging of anisotropic interactions provides significant improvement over the commonly used additivity approximation.

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The Electrostatic Interaction of Rigid, Globular Proteins with Arbitrary Charge Distributions

Cited by 36 publications

References 41 publications

Anisotropic protein–protein interactions due to ion binding

Anisotropic protein–protein interactions due to ion binding

Electrostatic Interactions between Peptides and the Molecular Chaperone DnaK

Forces between aqueous nonuniformly charged colloids from molecular simulation

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