Source:http://linkedlifedata.com/resource/pubmed/id/16044460
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2005-9-27
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pubmed:abstractText |
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 quantitative theory has not been developed, and such a theory is presented here. It is built on Kirkwood's idea that a salt ion has a repulsive interaction with an image charge inside a low dielectric cavity. Explicit treatment is given for the effect of other salt ions on the interaction between a salt ion and its image charge. When combined with the Debye-Hückel effect of salts on the solvation energy of protein charges (i.e., salting-in), the characteristic curve of protein solubility versus salt concentration is obtained. The theory yields a direct link between the salting-out effect and surface tension and is able to provide rationalizations for the effects of salt on the folding stability of several proteins.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
1097-0134
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pubmed:author | |
pubmed:copyrightInfo |
(c) 2005 Wiley-Liss, Inc.
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pubmed:issnType |
Electronic
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pubmed:day |
1
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pubmed:volume |
61
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
69-78
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:16044460-Animals,
pubmed-meshheading:16044460-Cold Temperature,
pubmed-meshheading:16044460-Hemoglobins,
pubmed-meshheading:16044460-Horses,
pubmed-meshheading:16044460-Ions,
pubmed-meshheading:16044460-Models, Chemical,
pubmed-meshheading:16044460-Nonlinear Dynamics,
pubmed-meshheading:16044460-Protein Denaturation,
pubmed-meshheading:16044460-Protein Folding,
pubmed-meshheading:16044460-Proteins,
pubmed-meshheading:16044460-Salts,
pubmed-meshheading:16044460-Solubility,
pubmed-meshheading:16044460-Static Electricity
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pubmed:year |
2005
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pubmed:articleTitle |
Interactions of macromolecules with salt ions: an electrostatic theory for the Hofmeister effect.
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pubmed:affiliation |
Department of Physics and Institute of Molecular Biophysics and School of Computational Science, Florida State University, Tallahassee 32306, USA. zhou@sb.fsu.edu
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, N.I.H., Extramural
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