| pubmed-article:8539615 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8539615 | lifeskim:mentions | umls-concept:C0005532 | lld:lifeskim |
| pubmed-article:8539615 | lifeskim:mentions | umls-concept:C0031453 | lld:lifeskim |
| pubmed-article:8539615 | lifeskim:mentions | umls-concept:C0041249 | lld:lifeskim |
| pubmed-article:8539615 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:8539615 | lifeskim:mentions | umls-concept:C0005036 | lld:lifeskim |
| pubmed-article:8539615 | lifeskim:mentions | umls-concept:C0007996 | lld:lifeskim |
| pubmed-article:8539615 | lifeskim:mentions | umls-concept:C0449911 | lld:lifeskim |
| pubmed-article:8539615 | pubmed:issue | 5246 | lld:pubmed |
| pubmed-article:8539615 | pubmed:dateCreated | 1996-2-8 | lld:pubmed |
| pubmed-article:8539615 | pubmed:abstractText | Cations bind to the pi face of an aromatic structure through a surprisingly strong, non-covalent force termed the cation-pi interaction. The magnitude and generality of the effect have been established by gas-phase measurements and by studies of model receptors in aqueous media. To first order, the interaction can be considered an electrostatic attraction between a positive charge and the quadrupole moment of the aromatic. A great deal of direct and circumstantial evidence indicates that cation-pi interactions are important in a variety of proteins that bind cationic ligands or substrates. In this context, the amino acids phenylalanine (Phe), tyrosine (Tyr), and tryptophan (Trp) can be viewed as polar, yet hydrophobic, residues. | lld:pubmed |
| pubmed-article:8539615 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8539615 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:8539615 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8539615 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8539615 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:8539615 | pubmed:issn | 0036-8075 | lld:pubmed |
| pubmed-article:8539615 | pubmed:author | pubmed-author:DoughertyD... | lld:pubmed |
| pubmed-article:8539615 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8539615 | pubmed:day | 12 | lld:pubmed |
| pubmed-article:8539615 | pubmed:volume | 271 | lld:pubmed |
| pubmed-article:8539615 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8539615 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8539615 | pubmed:pagination | 163-8 | lld:pubmed |
| pubmed-article:8539615 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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| pubmed-article:8539615 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8539615 | pubmed:articleTitle | Cation-pi interactions in chemistry and biology: a new view of benzene, Phe, Tyr, and Trp. | lld:pubmed |
| pubmed-article:8539615 | pubmed:affiliation | Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena 91125, USA. | lld:pubmed |
| pubmed-article:8539615 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8539615 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:8539615 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:8539615 | pubmed:publicationType | Review | lld:pubmed |
| pubmed-article:8539615 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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