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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Ion Specificity and Nonmonotonic Protein Solubility from Salt Entropy.
Modeling the Influence of Salt on the Hydrophobic Effect and Protein Fold Stability
TLDR
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.
Studying salt effects on protein stability using ribonuclease t1 as a model system.
Do soft anions promote protein denaturation through binding interactions? A case study using ribonuclease A
TLDR
Salt-induced perturbations to the protein folding free energy were determined using differential scanning calorimetry and the results demonstrate that the addition of sodium iodide and sodium thiocyanate significantly decreases the melting temperature of the protein.
The effect of lithium ions on the hydrophobic effect: does lithium affect hydrophobicity differently than other ions?
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 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.
The effect of monovalent cations on the collective dynamics of water and on a model protein
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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