| pubmed-article:3611088 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3611088 | lifeskim:mentions | umls-concept:C0020291 | lld:lifeskim |
| pubmed-article:3611088 | lifeskim:mentions | umls-concept:C0008742 | lld:lifeskim |
| pubmed-article:3611088 | lifeskim:mentions | umls-concept:C0019568 | lld:lifeskim |
| pubmed-article:3611088 | lifeskim:mentions | umls-concept:C1521991 | lld:lifeskim |
| pubmed-article:3611088 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
| pubmed-article:3611088 | lifeskim:mentions | umls-concept:C0887819 | lld:lifeskim |
| pubmed-article:3611088 | pubmed:issue | 22 | lld:pubmed |
| pubmed-article:3611088 | pubmed:dateCreated | 1987-9-17 | lld:pubmed |
| pubmed-article:3611088 | pubmed:abstractText | The hydrolysis of a set of 28 X-phenyl hippurates by chymotrypsin was investigated. From the derived Km and kcat values a quantitative structure-activity relationship was developed. This equation shows that para substituents correlated by sigma- display only an electronic effect on the formation of the ES complex whereas meta hydrophobic substituents show a hydrophobic interaction correlated by pi in addition to their electronic effect. Meta polar substituents avoid contact with the enzyme and show only electronic effects on Km. Using the x-ray crystallographic coordinates for chymotrypsin and computer graphics, a model was constructed which is used to interpret the quantitative structure-activity relationship. As with a number of previously reported examples, we have found that when polar substituents have the option of binding to hydrophobic space or remaining in the aqueous phase they follow the latter possibility. | lld:pubmed |
| pubmed-article:3611088 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3611088 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3611088 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3611088 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:3611088 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3611088 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3611088 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3611088 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3611088 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:3611088 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:3611088 | pubmed:author | pubmed-author:MorgensternLL | lld:pubmed |
| pubmed-article:3611088 | pubmed:author | pubmed-author:HanschCC | lld:pubmed |
| pubmed-article:3611088 | pubmed:author | pubmed-author:LangridgeRR | lld:pubmed |
| pubmed-article:3611088 | pubmed:author | pubmed-author:RecanatiniMM | lld:pubmed |
| pubmed-article:3611088 | pubmed:author | pubmed-author:KleinT ETE | lld:pubmed |
| pubmed-article:3611088 | pubmed:author | pubmed-author:YangC ZCZ | lld:pubmed |
| pubmed-article:3611088 | pubmed:author | pubmed-author:SteinmetzWW | lld:pubmed |
| pubmed-article:3611088 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3611088 | pubmed:day | 5 | lld:pubmed |
| pubmed-article:3611088 | pubmed:volume | 262 | lld:pubmed |
| pubmed-article:3611088 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3611088 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3611088 | pubmed:pagination | 10767-72 | lld:pubmed |
| pubmed-article:3611088 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
| pubmed-article:3611088 | pubmed:meshHeading | pubmed-meshheading:3611088-... | lld:pubmed |
| pubmed-article:3611088 | pubmed:meshHeading | pubmed-meshheading:3611088-... | lld:pubmed |
| pubmed-article:3611088 | pubmed:meshHeading | pubmed-meshheading:3611088-... | lld:pubmed |
| pubmed-article:3611088 | pubmed:meshHeading | pubmed-meshheading:3611088-... | lld:pubmed |
| pubmed-article:3611088 | pubmed:meshHeading | pubmed-meshheading:3611088-... | lld:pubmed |
| pubmed-article:3611088 | pubmed:meshHeading | pubmed-meshheading:3611088-... | lld:pubmed |
| pubmed-article:3611088 | pubmed:meshHeading | pubmed-meshheading:3611088-... | lld:pubmed |
| pubmed-article:3611088 | pubmed:meshHeading | pubmed-meshheading:3611088-... | lld:pubmed |
| pubmed-article:3611088 | pubmed:meshHeading | pubmed-meshheading:3611088-... | lld:pubmed |
| pubmed-article:3611088 | pubmed:meshHeading | pubmed-meshheading:3611088-... | lld:pubmed |
| pubmed-article:3611088 | pubmed:year | 1987 | lld:pubmed |
| pubmed-article:3611088 | pubmed:articleTitle | Chymotrypsin hydrolysis of X-phenyl hippurates. A quantitative structure-activity relationship and molecular graphics analysis. | lld:pubmed |
| pubmed-article:3611088 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3611088 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:3611088 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
