Hofmeister series

The kinetics - that is, the ease with which cations and (more pronounced) anions will be exchanged-follows the so-called Hofineister (lyotropic) series of preferential adsorption of ions on clay particles. The ions on the left will be more easily exchanged by ions positioned further right, than vice versa (Kunz et al., 2004)  

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Note Some of Grahame s values for and included in this table. For a common cation, the sequence of anions in order of increasing adsorption is similar to that of the Hofmeister series in coagulation studies, and it is evident that specific adsorption properties are involved. 

Cacace M G, Landau E M and Ramsden J J 1997 The Hofmeister series salt and solvent effects on interfacial phenomena Q. Rev. Biophys. 30 241-78... 

S ts can be used to precipitate proteins by salting out effects. The effectiveness of various salts is determined by the Hofmeister series, with anions being effective in the order citrate > PO4" > SO4" > CH3COO > Cl > NO3 , and cations according to NH4 > > Na ... 

The order of cations and anions regarding these structure breaking and making properties is related to their position in the lyotropic or Hofmeister series, such as... 

J.M. Roberts, A.R. Diaz, D.T. Fortin, J.M. Friedle and S.D. Piper, Influence of the Hofmeister series on the retention of amines in reversed-phase liquid chromatography, Anal. Chem., 74 (2002) 4927-4932. 

With the help of selectivity coefficients, such as in Eqs. (4.51) and (4.52) a general order of affinity can be given. For most clays the Hofmeister series (the same series as was given in Eq. (2.17) for the affinity of ions to oxide surfaces)... 

A number of studies have reported the abilities of different eluting salts to produce both different resolution and different selectivities.17 23 As expected, polyvalent ions are stronger eluters than monovalent ions. Some studies have suggested a correlation between eluting ability and ranking in the Hofmeister series. Others fail to observe this correlation, but nevertheless note differences in elution behavior. Overall, it is impossible to predict which eluting ions, if any, may produce a... 

An empirically derived relationships that describes the systematic effects of different neutral salts on the solubility of proteins. Collins and Washabaugh indicate that the order of ionic species eluding from a Sephadex G-10 column corresponds to the known order of effectiveness ions in the Hofmeister series on protein solubility ... 

METABOLIC CHANNELING CHAOTROPIC AGENTS HOFMEISTER SERIES KOSMOTROPES... 

HOFMEISTER SERIES CHAOTROPIC AGENTS KOSMOTROPES Hofstee plot,... 

COOPERATIVITY ALLOSTERISM INDUCED FIT MODEL MONOD-WYMAN-CHANGEUX MODEL INDEPENDENT BINDING LINKED FUNCTIONS ADAIR EQUATION POSITIVE COOPERATIVITY NEGATIVE COOPERATIVITY KOSMOTROPES CHAOTROPIC AGENTS HOFMEISTER SERIES Kp, Kq, K .. . ... 

Substances destroying the water structure, fhe so-called chao-tropic substances such as urea, guanidinium hydrochlorid, or some organic solvents such as mefhanol, efhanol, or acetonitrile, suppress hydrophobic interactions. Ions also alter the water structure. The power of destruction of water structure is given by the Hofmeister series ... 

Differences in both the charge density and the hydration of ions determine the Hofmeister series (lyotropic series).91... 

COAGULATION (Hofmeister Series). A definite order of arrangement of anions and cations according lo their powers of coagulation when their salts are added in quantity lo lyophilic sols. Thus, the order of cations... 

The retention caused by different salts in equal concentration is in accordance with the Hofmeister series. The higher the molar surface tension increment of a salt, the greater is its effect on protein retention 55). Higher column temperatures produce prolonged retention in HIC, in contrast to RPC where retention decreases with increasing temperature56). 

A summary of the transition temperatures of RNase in the presence of a variety of electrolytes is given in Table XX 361, 362). The effects of the usual salts follow the Hofmeister series. The remarkable difference in denaturing power of the various guanidinium salts is quite general. The sulfate actually tends to stabilize slightly while the thiocyanate is a more powerful denaturant than the chloride. Irreversible denaturation is markedly inhibited by spermine 363). There is no clear correlation between stabilizing effects and the complex inhibition curves obtained by Wold (see Section VI,E,2). 

Stability of an enzyme is usually understood to mean temperature stability, although inhibitors, oxygen, an unsuitable pH value, or other factors such as mechanical stress or shear can decisively influence stability (Chapter 17). The thermal stability of a protein, often employed in protein biochemistry, is characterized by the melting temperature Tm, the temperature at which a protein in equilibrium between native (N) and unfolded (U) species, N U, is half unfolded (Chapter 17, Section 17.2). The melting temperature of a protein is influenced on one hand by its amino acid sequence and the number of disulfide bridges and salt pairs, and on the other hand by solvent, added salt type, and added salt concentration. Protein structural stability was found to correlate also with the Hofmeister series (Chapter 3, Section 3.4 Hofmeister, 1888 von Hippel, 1964 Kaushik, 1999) [Eq. (2.18)]. 

Figure 8.6 Hofmeister series of kosmotropic and chaotropic ions.

Building Quantitative Models for the Hofmeister Series and Cohn-Edsall and Setschenow Equations... 

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