The structure and dipole moment of globular proteins in solution and crystalline states: Use of NMR and X-ray databases for the numerical calculation of dipole moment

Takashima, Shiro

doi:10.1002/1097-0282(20010405)58:4<398::aid-bip1016>3.0.co;2-9

Cited by 14 publications

(10 citation statements)

References 26 publications

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“…Direct interactions include short-range repulsive forces, which control steric excluded volume effects, reflecting the shape of the protein, van der Waals dispersion forces, and electrostatic forces associated with pH-dependent electric charges and higher electrostatic multipoles carried by the protein residues [7]. Other, effective, interactions depend on the degree of coarse-graining in the statistical description and result from the tracing out of microscopic degrees of freedom associated with the solvent and added electrolyte, i.e.…”

Section: Introductionmentioning

confidence: 99%

Nonmonotonic variation with salt concentration of the second virial coefficient in protein solutions

et al. 2003

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The osmotic virial coefficient B 2 of globular protein solutions is calculated as a function of added salt concentration at fixed pH by computer simulations of the "primitive model". The salt and counter-ions as well as a discrete charge pattern on the protein surface are explicitly incorporated. For parameters roughly corresponding to lysozyme, we find that B 2 first decreases with added salt concentration up to a threshold concentration, then increases to a maximum, and then decreases again upon further raising the ionic strength.Our studies demonstrate that the existence of a discrete charge pattern on the protein surface profoundly influences the effective interactions and that nonlinear Poisson Boltzmann and Derjaguin-Landau-Verwey-Overbeek (DLVO) theory fail for large ionic strength. The observed non-monotonicity of B 2 is compared to experiments. Implications for protein crystallization are discussed.

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Section: Introductionmentioning

confidence: 99%

Nonmonotonic variation with salt concentration of the second virial coefficient in protein solutions

et al. 2003

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“…Proteins have the unusually large dipole moment in comparison with the dipole moment of water molecules. For HEWL molecules it is equal to 121 D (Takashima, 2001). When the pH of the proteins solutions is outside of their isoelectric point the attractive dipole-dipole interactions between proteins are partially balanced by the repulsive interactions between their net charges.…”

Section: (Ct) = A(c) [T -T P (C)] -(C)mentioning

confidence: 99%

A comparison of the activation energy of viscous flow for hen egg-white lysozyme obtained on the basis of different models of viscosity for glass-forming liquids

Monkos¹

2011

Current Topics in Biophysics

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The paper presents the results of viscosity determinations on aqueous solutions of hen egg-white lysozyme at a wide range of concentrations and at temperatures ranging from 5 o C to 55 o C. On the basis of these measurements and different models of viscosity for glass-forming liquids, the activation energy of viscous flow for solutions and the studied protein, at different temperatures, was calculated. The analysis of the results obtained shows that the activation energy monotonically decreases with increasing temperature both for solutions and the studied protein. The numerical values of the activation energy for lysozyme, calculated on the basis of discussed models, are very similar in the range of temperatures from 5 o C to 35 o C.

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“…Conformational movement of the protein, for example, as the result of binding a substrate, can lead to a change in the overall dipole of the protein [7] which can be measured by impedance biosensors: impedance changes produced by binding of target molecules to receptor molecules immobilised on the surface of microelectrodes [8].…”

Section: Impedance Biosensingmentioning

confidence: 99%

Novel Bioimpedance Sensor for Glucose Recognition

Lumbroso

Naas

Beitel

et al. 2007

2007 International Symposium on Signals, Systems and Electronics

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The structure and dipole moment of globular proteins in solution and crystalline states: Use of NMR and X-ray databases for the numerical calculation of dipole moment

Cited by 14 publications

References 26 publications

Nonmonotonic variation with salt concentration of the second virial coefficient in protein solutions

Nonmonotonic variation with salt concentration of the second virial coefficient in protein solutions

A comparison of the activation energy of viscous flow for hen egg-white lysozyme obtained on the basis of different models of viscosity for glass-forming liquids

Novel Bioimpedance Sensor for Glucose Recognition

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