| pubmed-article:11162427 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11162427 | lifeskim:mentions | umls-concept:C0021756 | lld:lifeskim |
| pubmed-article:11162427 | lifeskim:mentions | umls-concept:C0041249 | lld:lifeskim |
| pubmed-article:11162427 | lifeskim:mentions | umls-concept:C0016315 | lld:lifeskim |
| pubmed-article:11162427 | lifeskim:mentions | umls-concept:C0598629 | lld:lifeskim |
| pubmed-article:11162427 | lifeskim:mentions | umls-concept:C0009085 | lld:lifeskim |
| pubmed-article:11162427 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:11162427 | pubmed:dateCreated | 2001-2-22 | lld:pubmed |
| pubmed-article:11162427 | pubmed:abstractText | The single tryptophan at position 121 of human interleukin-2 (IL-2) can form an NH-pi hydrogen bond with Phe 117 involving the indole nitrogen and the benzene aromatic ring. At pH 5.5, this type of aromatic interaction results in a fluorescence quantum yield three-fold lower than that of a fully solvent exposed tryptophan. At pH 2.1, IL-2 forms a compact denatured state with twice the emission intensity of the native protein. Global analysis of time-resolved fluorescence emission at multiple emission wavelengths shows that native and acid-denatured IL-2 can be described by four decay components. The fractional amplitudes of the shortest sub-nanosecond lifetimes are higher in the native state, suggesting rapid quenching due to the NH-pi hydrogen bond. In the denatured state, longer lifetimes have greater fractional amplitudes, indicating a smaller population of hydrogen-bonded species. Electrostatic-dipolar relaxation of the tryptophan microenvironment upon excitation is greater in the native-state of IL-2 than the acid-denatured state. This suggests that acid-denaturation sequesters Trp 121 from polar residues, while maintaining an interaction with Phe 117. This is consistent with the model of secondary structure preservation and hydrophobic clustering in molten-globule intermediates. | lld:pubmed |
| pubmed-article:11162427 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11162427 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11162427 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11162427 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11162427 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11162427 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11162427 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11162427 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11162427 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:11162427 | pubmed:issn | 0006-291X | lld:pubmed |
| pubmed-article:11162427 | pubmed:author | pubmed-author:BrandLL | lld:pubmed |
| pubmed-article:11162427 | pubmed:author | pubmed-author:NandaVV | lld:pubmed |
| pubmed-article:11162427 | pubmed:author | pubmed-author:LiangS MSM | lld:pubmed |
| pubmed-article:11162427 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11162427 | pubmed:day | 29 | lld:pubmed |
| pubmed-article:11162427 | pubmed:volume | 279 | lld:pubmed |
| pubmed-article:11162427 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11162427 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11162427 | pubmed:pagination | 770-8 | lld:pubmed |
| pubmed-article:11162427 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:11162427 | pubmed:meshHeading | pubmed-meshheading:11162427... | lld:pubmed |
| pubmed-article:11162427 | pubmed:meshHeading | pubmed-meshheading:11162427... | lld:pubmed |
| pubmed-article:11162427 | pubmed:meshHeading | pubmed-meshheading:11162427... | lld:pubmed |
| pubmed-article:11162427 | pubmed:meshHeading | pubmed-meshheading:11162427... | lld:pubmed |
| pubmed-article:11162427 | pubmed:meshHeading | pubmed-meshheading:11162427... | lld:pubmed |
| pubmed-article:11162427 | pubmed:meshHeading | pubmed-meshheading:11162427... | lld:pubmed |
| pubmed-article:11162427 | pubmed:meshHeading | pubmed-meshheading:11162427... | lld:pubmed |
| pubmed-article:11162427 | pubmed:meshHeading | pubmed-meshheading:11162427... | lld:pubmed |
| pubmed-article:11162427 | pubmed:meshHeading | pubmed-meshheading:11162427... | lld:pubmed |
| pubmed-article:11162427 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:11162427 | pubmed:articleTitle | Hydrophobic clustering in acid-denatured IL-2 and fluorescence of a Trp NH-pi H-bond. | lld:pubmed |
| pubmed-article:11162427 | pubmed:affiliation | Department of Biology, Johns Hopkins University, Baltimore, Maryland 21218, USA. | lld:pubmed |
| pubmed-article:11162427 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11162427 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11162427 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11162427 | lld:pubmed |
