| pubmed-article:7797251 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7797251 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:7797251 | lifeskim:mentions | umls-concept:C0242506 | lld:lifeskim |
| pubmed-article:7797251 | pubmed:issue | 2-3 | lld:pubmed |
| pubmed-article:7797251 | pubmed:dateCreated | 1995-8-3 | lld:pubmed |
| pubmed-article:7797251 | pubmed:abstractText | The human class I major histocompatibility complex (MHC) encoded molecule HLA-A2 loaded with the high-affinity peptide GILGRVFTL (p790), was studied by means of steady-state and picosecond fluorescence intensity and fluorescence anisotropy methods. The large number of tryptophan residues (W) (10 W/heavy chain, 2 W/beta 2m) as well as their fluorescence sensitivity to the microenvironment, determine the emission of the studied complex. The HLA-A2/peptide complex exhibits a considerable static inhomogeneous broadening (IB) of the W electronic spectra, which results in a dependence of the steady-state fluorescence spectrum on the excitation wavelength. The high concentration of W's chromophores and the spectral IB cause a directed non-radiative migration of electronic excitation energy by Foerster's mechanism from 'blue' W residues to 'red' ones. This phenomenon manifests itself in a nanosecond fluorescence spectral shift and an accelerated fluorescence depolarization at the red edge of the emission spectrum. Selective excitation at the red edge of the W absorption band (310 nm) provided a space selective reduction in the number of excited chromophores and enabled resolution of the emission of the 'red' subset of the protein's tryptophans. This avoided the non-radiative homo-energy transfer and enabled to study the fluorescence anisotropy decay kinetics of these residues without a distortion by the energy transfer (ET) process. Under these experimental conditions the fluorescence anisotropy decays practically from the limiting anisotropy value (0.3) for W in a bi-exponential process. The longer decay constant has a value larger than that expected for a global rotation of the HLA-A2/peptide complex suggesting that the protein molecules exist in an oligomeric form.(ABSTRACT TRUNCATED AT 250 WORDS) | lld:pubmed |
| pubmed-article:7797251 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7797251 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7797251 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7797251 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7797251 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7797251 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7797251 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7797251 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:7797251 | pubmed:issn | 0165-2478 | lld:pubmed |
| pubmed-article:7797251 | pubmed:author | pubmed-author:PechtII | lld:pubmed |
| pubmed-article:7797251 | pubmed:author | pubmed-author:StromingerJ... | lld:pubmed |
| pubmed-article:7797251 | pubmed:author | pubmed-author:HaasEE | lld:pubmed |
| pubmed-article:7797251 | pubmed:author | pubmed-author:RobbinsPP | lld:pubmed |
| pubmed-article:7797251 | pubmed:author | pubmed-author:GakamskyD MDM | lld:pubmed |
| pubmed-article:7797251 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7797251 | pubmed:volume | 44 | lld:pubmed |
| pubmed-article:7797251 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7797251 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7797251 | pubmed:pagination | 195-201 | lld:pubmed |
| pubmed-article:7797251 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:7797251 | pubmed:meshHeading | pubmed-meshheading:7797251-... | lld:pubmed |
| pubmed-article:7797251 | pubmed:meshHeading | pubmed-meshheading:7797251-... | lld:pubmed |
| pubmed-article:7797251 | pubmed:meshHeading | pubmed-meshheading:7797251-... | lld:pubmed |
| pubmed-article:7797251 | pubmed:meshHeading | pubmed-meshheading:7797251-... | lld:pubmed |
| pubmed-article:7797251 | pubmed:meshHeading | pubmed-meshheading:7797251-... | lld:pubmed |
| pubmed-article:7797251 | pubmed:meshHeading | pubmed-meshheading:7797251-... | lld:pubmed |
| pubmed-article:7797251 | pubmed:meshHeading | pubmed-meshheading:7797251-... | lld:pubmed |
| pubmed-article:7797251 | pubmed:meshHeading | pubmed-meshheading:7797251-... | lld:pubmed |
| pubmed-article:7797251 | pubmed:meshHeading | pubmed-meshheading:7797251-... | lld:pubmed |
| pubmed-article:7797251 | pubmed:meshHeading | pubmed-meshheading:7797251-... | lld:pubmed |
| pubmed-article:7797251 | pubmed:meshHeading | pubmed-meshheading:7797251-... | lld:pubmed |
| pubmed-article:7797251 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7797251 | pubmed:articleTitle | Selective steady-state and time-resolved fluorescence spectroscopy of an HLA-A2-peptide complex. | lld:pubmed |
| pubmed-article:7797251 | pubmed:affiliation | Department of Chemical Immunology, Weizmann Institute of Science, Rehovot, Israel. | lld:pubmed |
| pubmed-article:7797251 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7797251 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:7797251 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
