Lyotropy

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Lyotropy (from

aqueous solutions
.

History

salt out proteins.[1]

Because of the positive charge of lysozyme, the original series turned out to be different than the series for most proteins. Thus, the series can change depending on the protein in solution and the concentrations of the ions in solution. Lyotropy- like the Hofmeister series- classifies ions and their abilities to salt in/ salt out proteins.

In 1936,

colloids. Lyotropic numbers, Nlyo, based on this work appear to be related to the charge density of the ions.[2]

Lyotropic activity also influences swelling of gels, surface tension, rate of saponification processes, viscosity of salt solutions, and heats of hydration.[3][4]

Ion pairing equilibria

The current understanding of ion-pairing equilibria in an aqueous environment can also be traced to the Eigen-Tamm model that introduced the use of two equilibria states for ion pairs: the

cation ion-pairing in seawater.[6]

This ion-specific behavior was also elucidated through Collin's Law of Matching Water Affinities that describes the strength of ion-pairing in terms of ion size and

ion-pairing involve molecular dynamic simulations and ab initio calculations that often incorporate polarizable continuum solvent models.[9]

Implications

Following the law of matching water affinities,

potassium ion (K+) will prefer a sulfonate, which has important partitioning effects in biological systems.[10] Protein solubility depends on pH and salt concentration, where small changes in the local environment can lead to Hofmeister series reversals.[9]

In aqueous solutions of

pi-stacking interactions.[12]

In carbohydrates, electrostatic and ion pairing are the dominant mechanisms for molecular interactions. Modern computational approaches in salt bridge formation in protein demonstrate that the favorable arginine-arginine pairing (i.e. conserved arginine) is due to reduction in electrostatic repulsion.[12]

Electrolyotropy

Electrolyotropy incorporates Donnan-potential spatial gradients and ion-specific pairing, and is used to determine the distribution of the ions and electric potential by modeling charges as being either fixed or free.[13] A canonical example is a surface-tethered polyelectrolyte brush with a variety of different fixed charged groups interacting with free ions and ion-pairs to minimize Gibbs free energy.

Using streaming current measurements in a

mucosal tissue.[13][15]

References

  1. ISBN 978-981-4271-57-8
    .
  2. PMID 34976339
    .
  3. doi:10.1021/cr60066a001
    .
  4. doi:10.1002/recl.19590780302
    .
  5. ^
    PMID 26437440
    .
  6. doi:10.4319/lo.1969.14.5.0686
    .
  7. S2CID 206613894
    .
  8. PMID 17091929
    .
  9. ^
    PMID 25494656
    .
  10. PMID 18973869
    .
  11. PMID 18220363
    .
  12. ^
    PMID 19354258
    .
  13. ^
    doi:10.1016/j.colcom.2017.08.002
    .
  14. hdl:2066/175420
    .
  15. doi:10.1002/mats.201700079
    .
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