| pubmed-article:11928507 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11928507 | lifeskim:mentions | umls-concept:C0026336 | lld:lifeskim |
| pubmed-article:11928507 | lifeskim:mentions | umls-concept:C1522290 | lld:lifeskim |
| pubmed-article:11928507 | lifeskim:mentions | umls-concept:C1706211 | lld:lifeskim |
| pubmed-article:11928507 | lifeskim:mentions | umls-concept:C0679083 | lld:lifeskim |
| pubmed-article:11928507 | lifeskim:mentions | umls-concept:C0007961 | lld:lifeskim |
| pubmed-article:11928507 | lifeskim:mentions | umls-concept:C1546426 | lld:lifeskim |
| pubmed-article:11928507 | lifeskim:mentions | umls-concept:C1548280 | lld:lifeskim |
| pubmed-article:11928507 | pubmed:dateCreated | 2002-4-3 | lld:pubmed |
| pubmed-article:11928507 | pubmed:abstractText | A new method for considering solvation when calculating electrostatics for protein docking is proposed. The solvent-exposed charges are attenuated by induced solvent polarization charges. Modified charges are pre-calculated and the correction doesn't affect the speed of the actual simulation. The new Screened Charge Electrostatic Model (SChEM) results in an improved discrimination of near-native solutions from false positives in docking simulations as compared to conventional 'non-solvated' charge assignment. A series of protein-protein complexes were analyzed by running automated rigid-body Monte-Carlo docking simulations using the 3-D coordinates of the unbound components. In all but one case, the use of solvation screened charges for electrostatic calculations helped to improve the rank of the near-native solution after rigid-body simulations. The SChEM also drastically improved the results of the subsequent refinement of the interface side-chains. In all cases the final lowest energy solution was found within 3.0 A r.m.s.d. of the crystal structure. | lld:pubmed |
| pubmed-article:11928507 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11928507 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11928507 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11928507 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11928507 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11928507 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11928507 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11928507 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11928507 | pubmed:issn | 1793-5091 | lld:pubmed |
| pubmed-article:11928507 | pubmed:author | pubmed-author:TotrovMaximM | lld:pubmed |
| pubmed-article:11928507 | pubmed:author | pubmed-author:AbagyanRubenR | lld:pubmed |
| pubmed-article:11928507 | pubmed:author | pubmed-author:Fernandez-Rec... | lld:pubmed |
| pubmed-article:11928507 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11928507 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11928507 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11928507 | pubmed:pagination | 552-63 | lld:pubmed |
| pubmed-article:11928507 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
| pubmed-article:11928507 | pubmed:meshHeading | pubmed-meshheading:11928507... | lld:pubmed |
| pubmed-article:11928507 | pubmed:meshHeading | pubmed-meshheading:11928507... | lld:pubmed |
| pubmed-article:11928507 | pubmed:meshHeading | pubmed-meshheading:11928507... | lld:pubmed |
| pubmed-article:11928507 | pubmed:meshHeading | pubmed-meshheading:11928507... | lld:pubmed |
| pubmed-article:11928507 | pubmed:meshHeading | pubmed-meshheading:11928507... | lld:pubmed |
| pubmed-article:11928507 | pubmed:meshHeading | pubmed-meshheading:11928507... | lld:pubmed |
| pubmed-article:11928507 | pubmed:meshHeading | pubmed-meshheading:11928507... | lld:pubmed |
| pubmed-article:11928507 | pubmed:meshHeading | pubmed-meshheading:11928507... | lld:pubmed |
| pubmed-article:11928507 | pubmed:meshHeading | pubmed-meshheading:11928507... | lld:pubmed |
| pubmed-article:11928507 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:11928507 | pubmed:articleTitle | Screened charge electrostatic model in protein-protein docking simulations. | lld:pubmed |
| pubmed-article:11928507 | pubmed:affiliation | Department of Molecular Biology, Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA. jfrecio@scripps.edu | lld:pubmed |
| pubmed-article:11928507 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11928507 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
