On the molecular mechanism of ion specific Hofmeister series

On the molecular mechanism of ion specific Hofmeister series. Xie, W., J., Liu, C., Yang, L., & Gao, Y., Q. Science China Chemistry, 57:36-47, 2014.

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On the molecular mechanism of ion specific Hofmeister series [link]

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Hofmeister series ranks the ability of salt ions in influencing a\nvariety of properties and processes in aqueous solutions. In this\nreview, we reexamine how these ions and some other small molecules\naffect water structure and thermodynamic properties, such as surface\ntension and protein backbone solvation. We illustrate the difficulties\nin interpreting the thermodynamic information based on structural and\ndynamic arguments. As an alternative, we show that the solvation\nproperties of ions and proteins/small molecules can be used to explain\nthe salt effects on the thermodynamic properties of the solutions. Our\nanalysis shows that the often neglected cation-anion cooperativity plays\na very important role in these effects. We also argue that the change of\nhydrogen donor/acceptor equilibrium by added cosolutes/cosolvents can be\nused to explain their effects on protein secondary structure\ndenaturation/protection: those increase hydrogen donor concentrations\nsuch as urea and salts with strongly solvated cations/weakly hydrated\nanions tend to dissolve protein backbone acting as secondary structure\ndenaturants, whereas those lack of hydrogen donors but rich in acceptors\nhave the opposite effect.

@article{
 title = {On the molecular mechanism of ion specific Hofmeister series},
 type = {article},
 year = {2014},
 keywords = {Hofmeister series,hydrogen donor/acceptor equilibrium,ion cooperativity,protein denaturant,protein protectant,salt effects,surface tension},
 pages = {36-47},
 volume = {57},
 websites = {http://download.springer.com/static/pdf/815/art%253A10.1007%252Fs11426-013-5019-1.pdf?originUrl=http%3A%2F%2Flink.springer.com%2Farticle%2F10.1007%2Fs11426-013-5019-1&token2=exp=1465142065~acl=%2Fstatic%2Fpdf%2F815%2Fart%25253A10.1007%25252Fs11426-013-501},
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 created = {2017-09-28T14:05:00.489Z},
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 last_modified = {2020-08-12T04:26:59.143Z},
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 citation_key = {Xie2014},
 source_type = {Journal Article},
 language = {English},
 notes = {Sp. Iss. SI<br/>281OE<br/>Times Cited:6<br/>Cited References Count:99},
 private_publication = {false},
 abstract = {Hofmeister series ranks the ability of salt ions in influencing a\nvariety of properties and processes in aqueous solutions. In this\nreview, we reexamine how these ions and some other small molecules\naffect water structure and thermodynamic properties, such as surface\ntension and protein backbone solvation. We illustrate the difficulties\nin interpreting the thermodynamic information based on structural and\ndynamic arguments. As an alternative, we show that the solvation\nproperties of ions and proteins/small molecules can be used to explain\nthe salt effects on the thermodynamic properties of the solutions. Our\nanalysis shows that the often neglected cation-anion cooperativity plays\na very important role in these effects. We also argue that the change of\nhydrogen donor/acceptor equilibrium by added cosolutes/cosolvents can be\nused to explain their effects on protein secondary structure\ndenaturation/protection: those increase hydrogen donor concentrations\nsuch as urea and salts with strongly solvated cations/weakly hydrated\nanions tend to dissolve protein backbone acting as secondary structure\ndenaturants, whereas those lack of hydrogen donors but rich in acceptors\nhave the opposite effect.},
 bibtype = {article},
 author = {Xie, Wen Jun and Liu, Chengwen and Yang, Lijiang and Gao, Yi Qin},
 doi = {10.1007/s11426-013-5019-1},
 journal = {Science China Chemistry}
}

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