Linked Life Data

8555224

Source:http://linkedlifedata.com/resource/pubmed/id/8555224

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1996-2-23
pubmed:abstractText
The ligand-induced conformational change of an active lysozyme derivative, Kyn62-lysozyme, in which Trp62 of hen egg-white lysozyme (EC 3.2.1.17) was selectively modified to kynurenine, was investigated by steady-state and time-resolved fluorescence spectroscopy. Kyn62 formed an intramolecular energy transfer donor-acceptor pair with a tryptophan residue as a donor. The energy transfer was related to the conformation of the active site. The spectral overlap integral (J) of the kynurenine-tryptophan pair is large as it was determined to be 4.92 x 10(-15) M-1 cm3. Time-resolved fluorescence properties of Kyn62-lysozyme and its complex with a trimer of N-acetyl-D-glucosamine [(GlcNAc)3] show that the energy donor is Trp28 or Trp111 in the hydrophobic matrix box of the free Kyn62-lysozyme. In the complex, it appears that the kynurenine residue drastically changed its orientation or approached closer to Trp108 to accept more efficiently the excitation energy from Trp108 on the binding of Kyn62-lysozyme with (GlcNAc)3.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
16
pubmed:volume
35
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
531-7
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Steady-state and time-resolved fluorescence studies on the ligand-induced conformational change in an active lysozyme derivative, Kyn62-lysozyme.
pubmed:affiliation
Institute of Biophysics, Faculty of Agriculture, Kyushu University, Fukuoka, Japan.
pubmed:publicationType
Journal Article, In Vitro