Interactions of macromolecules with salt ions: An electrostatic theory for the Hofmeister effect

@article{Zhou2005InteractionsOM,
  title={Interactions of macromolecules with salt ions: An electrostatic theory for the Hofmeister effect},
  author={Huan‐Xiang Zhou},
  journal={Proteins: Structure},
  year={2005},
  volume={61}
}
Salting‐out of proteins was discovered in the nineteenth century and is widely used for protein separation and crystallization. It is generally believed that salting‐out occurs because at high concentrations salts and the protein compete for solvation water. Debye and Kirkwood suggested ideas for explaining salting‐out (Debeye and MacAulay, Physik Z; 1925;131:22–29; Kirkwood, In: Proteins, amino acids and peptides as ions and dipolar ions. New York: Reinhold; 1943. p 586–622). However, a… 
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A continuum solvation based model is developed that relies on a traditional Poisson-Boltzmann term to describe the polar or electro- static effects of salt, and a surface area dependent term containing a salt concentration dependent microscopic surface tension function to capture the non-polar Hofmeister effects.
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The salting-out effect, which was considered to be secondary to electrostatic screening, is important for IDP sequences with moderate charged residues at physiological salt concentrations and is parameterized into a coarse-grained model using a set of Förster resonance energy transfer data.
Salt-Dependent Conformational Changes of Intrinsically Disordered Proteins.
TLDR
The salting-out effect, which was considered to be secondary to electrostatic screening, is important for IDP sequences with moderately charged residues at physiological salt concentrations, and the presented scheme is generally applicable to other computational models for capturing salt-dependent IDP conformations.
Biomolecular electrostatics and solvation: a computational perspective
TLDR
The solvation of biomolecules with a computational biophysics view toward describing the phenomenon is discussed, and the main focus lies on the computational aspect of the models.
Electrostatic Interactions in Protein Structure, Folding, Binding, and Condensation.
TLDR
This review will examine how charged side chains are spatially distributed in various types of proteins and how electrostatic interactions affect thermodynamic and kinetic properties of proteins.
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References

SHOWING 1-10 OF 51 REFERENCES
How ions affect the structure of water.
TLDR
Two main ideas captured here are that charge densities govern the interactions of ions with water, and that a balance of forces determines water structure: electrostatics (water's dipole interacting with ions) and hydrogen bonding (water interacting with neighboring waters).
Salting-In and Salting-Out of Hydrophobic Solutes in Aqueous Salt Solutions
We present results on the thermodynamic and structural aspects of the hydration of hydrophobic solutes in three tetramethylammonium [N(CH3)4+] salt solutions at various concentrations obtained from
How Hofmeister ion interactions affect protein stability.
The structure of aqueous guanidinium chloride solutions.
TLDR
The marked tendency of the guanidinium ions to stack parallel to their water-deficient surfaces indicates that the efficiency of this ion as a denaturant is due to its ability to simultaneously interact favorably with both water and hydrophobic side chains of proteins.
Theory of Solutions of Molecules Containing Widely Separated Charges with Special Application to Zwitterions
The electrical contribution to the chemical potential of an ion having an arbitrary charge distribution is calculated with the aid of the Debye‐Huckel theory. The calculation is based upon a general
The Hofmeister effect and the behaviour of water at interfaces.
TLDR
The first general, detailed qualitative molecular mechanism for the origins of ion-specific (Hofmeister) effects on the surface potential difference at an air-water interface is proposed; this mechanism suggests a simple model for the behaviour of water at all interfaces, regardless of whether the non-aqueous component is neutral or charged, polar or non-polar.
STUDIES IN THE PHYSICAL CHEMISTRY OF THE PROTEINS : VI. THE ACTIVITY COEFFICIENTS OF THE IONS IN CERTAIN OXYHEMOGLOBIN SOLUTIONS.
1. The solvent action of a neutral salt upon a protein, oxyhemoglobin, has been found identical to the solvent action of a neutral salt upon a bi-bivalent or uni-quadrivalent compound. 2. The
...
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