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Crystal Field Theory
To explain the observed behavior of transition metal complexes (such as colors), a model involving electrostatic interactions between the electrons from the ligands and the electrons in the unhybridized d orbitals of the central metal atom has been developed. This electrostatic model is crystal field theory (CFT). It helps to understand, interpret, and predict the colors, magnetic behavior, and some structures of coordination compounds of transition metals.
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The ionic strength of a solution is a quantitative way of expressing the total electrolyte concentration of a solution. This concept was first introduced in 1921 by two American physical chemists, Gilbert N. Lewis and Merle Randall, while describing the activity coefficient of strong electrolytes. During the calculation of ionic strength (I or μ), all the cations and anions are considered. However, the concentration (c) of an ion with a greater charge number (z) has a greater contribution...
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Colligative Properties of Electrolytes
The colligative properties of a solution depend only on the number, not on the identity, of solute species dissolved. The concentration terms in the equations for various colligative properties (freezing point depression, boiling point elevation, osmotic pressure) pertain to all solute species present in the solution. Nonelectrolytes dissolve physically without dissociation or any other accompanying process. Each molecule that dissolves yields one...
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The hemoglobin in the blood, the chlorophyll in green plants, vitamin B-12, and the catalyst used in the manufacture of polyethylene all contain coordination compounds. Ions of the metals, especially the transition metals, are likely to form complexes.
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The addition of an inert ionic compound increases the solubility of a sparingly soluble salt. For example, adding potassium nitrate to a saturated solution of calcium sulfate significantly enhances the solubility of calcium sulfate. Le Châtelier's principle cannot predict this shift in the equilibrium. Instead, this could be explained in terms of changes in the effective concentration of the ions in solution in the presence of added inert salt.
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Tetrahedral Complexes
Crystal field theory (CFT) is applicable to molecules in geometries other than octahedral. In octahedral complexes, the lobes of the dx2−y2 and dz2 orbitals point directly at the ligands. For tetrahedral complexes, the d orbitals remain in place, but with only four ligands located between the axes. None of the orbitals points directly at the tetrahedral ligands. However, the dx2−y2 and dz2 orbitals (along the Cartesian axes) overlap with the ligands less than the dxy,...
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Vibrational Spectra of a N719-Chromophore/Titania Interface from Empirical-Potential Molecular-Dynamics Simulation, Solvated by a Room Temperature Ionic Liquid
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Ionic strength-dependent changes in tentacular ion exchangers with variable ligand density. II. Functional

Rahul Bhambure1, James M Angelo2, Christopher M Gillespie3

  • 1Department of Chemical and Biomolecular Engineering, University of Delaware, Newark, DE, 19716, USA; National Chemical Laboratory, Pune, India.

Journal of Chromatography. A
|May 31, 2017
PubMed
Summary

Ligand density and ionic strength significantly impact protein adsorption and transport in cation-exchange sorbents. These factors influence binding capacities, transport rates, and affinities for proteins like lysozyme and monoclonal antibodies (mAbs).

Keywords:
Binding capacityIsocratic retentionLigand densityLysozymeMonoclonal antibodyUptake and elution

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Area of Science:

  • Biochemistry
  • Materials Science
  • Chemical Engineering

Background:

  • Protein adsorption and transport are critical in chromatography and bioseparations.
  • Understanding the influence of sorbent properties like ligand density is essential for optimizing these processes.

Purpose of the Study:

  • To investigate the effects of ligand density and ionic strength on protein adsorption and transport behavior.
  • To analyze the impact on binding capacities, transport rates, and affinities for different proteins.

Main Methods:

  • Studied protein adsorption and transport using tentacular cation-exchange sorbents.
  • Performed uptake and elution experiments with lysozyme, lactoferrin, and monoclonal antibodies (mAbs).
  • Quantified intraparticle protein diffusivities and correlated them with sorbent structural properties.

Main Results:

  • Decreasing uptake diffusivities were observed with increasing ligand density, linked to accessible porosity.
  • Increased ionic strength enhanced mass transfer during uptake, especially for larger proteins (lactoferrin, mAb) at high ligand densities.
  • Binding capacities varied: higher for lysozyme with increased ligand density, but complex for lactoferrin and mAb due to ionic strength-dependent porosity.

Conclusions:

  • Ligand density and ionic strength are key variables controlling protein behavior in cation-exchange sorbents.
  • Sorbent porosity and protein size/charge significantly mediate these effects.
  • Optimizing ligand density and ionic strength is crucial for effective protein separation and purification.