| pubmed-article:16044460 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16044460 | lifeskim:mentions | umls-concept:C0022023 | lld:lifeskim |
| pubmed-article:16044460 | lifeskim:mentions | umls-concept:C0037494 | lld:lifeskim |
| pubmed-article:16044460 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:16044460 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
| pubmed-article:16044460 | lifeskim:mentions | umls-concept:C0178735 | lld:lifeskim |
| pubmed-article:16044460 | lifeskim:mentions | umls-concept:C0871935 | lld:lifeskim |
| pubmed-article:16044460 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:16044460 | pubmed:dateCreated | 2005-9-27 | lld:pubmed |
| pubmed-article:16044460 | 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. | lld:pubmed |
| pubmed-article:16044460 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16044460 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16044460 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16044460 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16044460 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16044460 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16044460 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16044460 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16044460 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16044460 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:16044460 | pubmed:issn | 1097-0134 | lld:pubmed |
| pubmed-article:16044460 | pubmed:author | pubmed-author:ZhouHuan-Xian... | lld:pubmed |
| pubmed-article:16044460 | pubmed:copyrightInfo | (c) 2005 Wiley-Liss, Inc. | lld:pubmed |
| pubmed-article:16044460 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:16044460 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:16044460 | pubmed:volume | 61 | lld:pubmed |
| pubmed-article:16044460 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16044460 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16044460 | pubmed:pagination | 69-78 | lld:pubmed |
| pubmed-article:16044460 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
| pubmed-article:16044460 | pubmed:meshHeading | pubmed-meshheading:16044460... | lld:pubmed |
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| pubmed-article:16044460 | pubmed:meshHeading | pubmed-meshheading:16044460... | lld:pubmed |
| pubmed-article:16044460 | pubmed:meshHeading | pubmed-meshheading:16044460... | lld:pubmed |
| pubmed-article:16044460 | pubmed:meshHeading | pubmed-meshheading:16044460... | lld:pubmed |
| pubmed-article:16044460 | pubmed:meshHeading | pubmed-meshheading:16044460... | lld:pubmed |
| pubmed-article:16044460 | pubmed:meshHeading | pubmed-meshheading:16044460... | lld:pubmed |
| pubmed-article:16044460 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:16044460 | pubmed:articleTitle | Interactions of macromolecules with salt ions: an electrostatic theory for the Hofmeister effect. | lld:pubmed |
| pubmed-article:16044460 | 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 | lld:pubmed |
| pubmed-article:16044460 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16044460 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:16044460 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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