| pubmed-article:7756531 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7756531 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:7756531 | lifeskim:mentions | umls-concept:C0425245 | lld:lifeskim |
| pubmed-article:7756531 | lifeskim:mentions | umls-concept:C1880157 | lld:lifeskim |
| pubmed-article:7756531 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:7756531 | pubmed:dateCreated | 1995-6-26 | lld:pubmed |
| pubmed-article:7756531 | pubmed:abstractText | A scheme is presented for computing the electrophoretic mobility of proteins in free solution, accounting for the details of the protein shape and charge distribution. The method of Teubner is implemented using a boundary integral formulation within which the velocity distribution, the equilibrium electrical potential around the molecule, and the potential distribution due to the applied field are solved for numerically using the boundary element method. Good agreement of the numerical result is obtained for spheres with the corresponding semi-analytical specialization of Henry's analysis. For protein systems, the method is applied to lysozyme and ribonuclease A. In both cases, the predicted mobility tensors are fairly isotropic, with the resulting scalar mobilities being significantly smaller than for spheres of equal volume and net charge. Comparisons with previously published experimental results for ribonuclease show agreement to be excellent in the presence of a net charge, but poorer at the point of zero charge. The approach may be useful for evaluating approximate methods for estimating protein electrophoretic mobilities and for using electrophoretic measurements to obtain insight into charge distributions on proteins. | lld:pubmed |
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| pubmed-article:7756531 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7756531 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7756531 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:7756531 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7756531 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:7756531 | pubmed:issn | 0006-3495 | lld:pubmed |
| pubmed-article:7756531 | pubmed:author | pubmed-author:ChaeK SKS | lld:pubmed |
| pubmed-article:7756531 | pubmed:author | pubmed-author:LenhoffA MAM | lld:pubmed |
| pubmed-article:7756531 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7756531 | pubmed:volume | 68 | lld:pubmed |
| pubmed-article:7756531 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7756531 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7756531 | pubmed:pagination | 1120-7 | lld:pubmed |
| pubmed-article:7756531 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:7756531 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7756531 | pubmed:articleTitle | Computation of the electrophoretic mobility of proteins. | lld:pubmed |
| pubmed-article:7756531 | pubmed:affiliation | Department of Chemical Engineering, University of Delaware, Newark 19716, USA. | lld:pubmed |
| pubmed-article:7756531 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7756531 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
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