| pubmed-article:4046024 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:4046024 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:4046024 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:4046024 | lifeskim:mentions | umls-concept:C1441506 | lld:lifeskim |
| pubmed-article:4046024 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:4046024 | pubmed:dateCreated | 1985-10-30 | lld:pubmed |
| pubmed-article:4046024 | pubmed:abstractText | In this paper we present a classical treatment of electrostatic interactions in proteins. The protein is treated as a region of low dielectric constant with spherical charges embedded within it, surrounded by an aqueous solvent of high dielectric constant, which may contain a simple electrolyte. The complete analysis includes the effects of solvent screening, polarization forces, and self energies, which are related to solvation energies. Formulae, and sample calculations of forces and energies, are given for the special case of a spherical protein. Our analysis and model calculations point out that any consistent treatment of electrostatic interactions in proteins should account for the following. Solvent polarization is an important factor in the calculation of pairwise electrostatic interactions. Solvent polarization substantially affects both electrostatic energies and forces acting upon charges. No simple expression for the effective dielectric constant, Deff, can generally be valid, since Deff is a sensitive function of position. Solvent screening of pairwise interactions involving dipolar groups is less effective than the screening of charges. In fact for many interactions involving dipoles, solvent screening can be essentially ignored. The self energy of charges makes a large contribution to the total electrostatic energy of a protein. This must be compensated by specific interactions with other groups in the protein. Strategies for applying our analysis to proteins whose structures are known are discussed. | lld:pubmed |
| pubmed-article:4046024 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:4046024 | pubmed:language | eng | lld:pubmed |
| pubmed-article:4046024 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:4046024 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:4046024 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:4046024 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:4046024 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:4046024 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:4046024 | pubmed:issn | 0022-2836 | lld:pubmed |
| pubmed-article:4046024 | pubmed:author | pubmed-author:FineRR | lld:pubmed |
| pubmed-article:4046024 | pubmed:author | pubmed-author:HonigBB | lld:pubmed |
| pubmed-article:4046024 | pubmed:author | pubmed-author:GilsonM KMK | lld:pubmed |
| pubmed-article:4046024 | pubmed:author | pubmed-author:RashinAA | lld:pubmed |
| pubmed-article:4046024 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:4046024 | pubmed:day | 5 | lld:pubmed |
| pubmed-article:4046024 | pubmed:volume | 184 | lld:pubmed |
| pubmed-article:4046024 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:4046024 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:4046024 | pubmed:pagination | 503-16 | lld:pubmed |
| pubmed-article:4046024 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:4046024 | pubmed:meshHeading | pubmed-meshheading:4046024-... | lld:pubmed |
| pubmed-article:4046024 | pubmed:meshHeading | pubmed-meshheading:4046024-... | lld:pubmed |
| pubmed-article:4046024 | pubmed:meshHeading | pubmed-meshheading:4046024-... | lld:pubmed |
| pubmed-article:4046024 | pubmed:meshHeading | pubmed-meshheading:4046024-... | lld:pubmed |
| pubmed-article:4046024 | pubmed:meshHeading | pubmed-meshheading:4046024-... | lld:pubmed |
| pubmed-article:4046024 | pubmed:meshHeading | pubmed-meshheading:4046024-... | lld:pubmed |
| pubmed-article:4046024 | pubmed:year | 1985 | lld:pubmed |
| pubmed-article:4046024 | pubmed:articleTitle | On the calculation of electrostatic interactions in proteins. | lld:pubmed |
| pubmed-article:4046024 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:4046024 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:4046024 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:4046024 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:4046024 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:4046024 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:4046024 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:4046024 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:4046024 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:4046024 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:4046024 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:4046024 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:4046024 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:4046024 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:4046024 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:4046024 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:4046024 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:4046024 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:4046024 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:4046024 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:4046024 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:4046024 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:4046024 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:4046024 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:4046024 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:4046024 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:4046024 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:4046024 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:4046024 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:4046024 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:4046024 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:4046024 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:4046024 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:4046024 | lld:pubmed |
