Linked Life Data

9376355

Source:http://linkedlifedata.com/resource/pubmed/id/9376355

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
41
pubmed:dateCreated
1997-11-12
pubmed:abstractText
The binding of p7 nucleocapsid protein of type 1 human immunodeficiency virus (HIV-1) to various oligonucleotides and polynucleotides has been investigated by phosphorescence and optically detected magnetic resonance (ODMR) spectroscopy. The intrinsic spectroscopic probe used in these studies is the photoexcited triplet state of Trp37, which is associated with the C-terminal zinc finger of p7 and is its only tryptophan residue. Complex formation produces a red-shift of the phosphorescence 0, 0-band (DeltaE0,0) of Trp37 as well as a reduction of the zero field splitting (zfs) D parameter. Increases of -DeltaE0,0 (A < C < U < G <I) rank with increasing binding affinity to nucleic acid homooligomers (A approximately C < U < G approximately I). It is proposed that the magnitude of the shift reflects the extent of aromatic stacking interactions. We propose also that -DeltaD increases not only with increased aromatic stacking but also with the extent of charge transfer (CT) character admixed into the triplet state. The quantity DeltaD/DeltaE0,0 correlates with the electron affinity of the bases (G < A < C < U approximately T), suggesting that this quantity reflects the extent of CT character admixed with the triplet state by the aromatic stacking interaction. Also affected by nucleic acid binding of p7 are the kinetic parameters of Trp37. We find a selective increase in the relative populating rate, and of the decay rate constant of the Tx sublevel. In binding of p7 to either d(IT)2 or d(IT)4, two distinct sets of triplet states of Trp37 are resolved, suggesting the existence of specific nucleic acid binding modes of these heterooligomers.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
14
pubmed:volume
36
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
12506-18
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Binding of the nucleocapsid protein of type 1 human immunodeficiency virus to nucleic acids studied using phosphorescence and optically detected magnetic resonance.
pubmed:affiliation
Department of Chemistry, University of California, Davis, California 95616, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't