Linked Life Data

7032589

Source:http://linkedlifedata.com/resource/pubmed/id/7032589

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
25
pubmed:dateCreated
1982-3-13
pubmed:abstractText
Phosphorescence spectroscopy and optical detection of triplet state magnetic resonance (ODMR) spectroscopy have been used to characterize bases that contribute to the phosphorescence emission of Escherichia coli valine-specific transfer ribonucleic acid. When it is excited with 335-nm light, a short-lived phosphorescence with an origin near 435 nm is observed and is assigned to 4-thiouridine (s4U) at position 8 of the tRNA sequence. With excitation at 290-300 nm, a structured, long-lived phosphorescence is observed with an origin near 380 nm, in addition to the s4U phosphorescence. Comparison was made of the phosphorescence and ODMR spectra between Mg2+-containing and Mg2+-free tRNA samples. The s4U phosphorescence of the Mg2+-containing sample is more structured, and the peak is blue shifted relative to the Mg2+-free sample. Both samples give a single low-frequency (ca. 2.9 GHz) ODMR signal, but the high-frequency signal region (ca. 19-20 GHz) is structured. The Mg2+-containing sample has a partially resolved group of lines centered at 19.3 GHz, whereas the Mg2+-free sample has two broad bands centered at 19.2 and 20.0 gHz. The differences are attributed to effects of Mg2+ on the tRNA conformation. The ODMR signals observed by monitoring the long-lived phosphorescence are assigned to a pyrimidine nucleoside, possibly 5-(carboxy-methoxy)uridine in the anticodon.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
8
pubmed:volume
20
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
7295-301
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1981
pubmed:articleTitle
Optically detected magnetic resonance of the phosphorescent bases of Escherichia coli valine-specific transfer ribonucleic acid.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S.