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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1995-4-25
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pubmed:abstractText |
In the past year, a number of studies have demonstrated the utility of fluorescence resonance energy transfer as a technique for probing complex intermolecular interactions and for determining the spatial extension and geometrical characteristics of multicomponent structures composed of diverse molecular constituents, such as proteins, lipids, carbohydrates, nucleic acids, and even cells with viruses. The benefits of fluorescence resonance energy transfer are becoming increasingly evident to researchers who require measurements with high sensitivity, specificity, non-invasiveness, rapidity, and relative simplicity.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0958-1669
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
6
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
103-10
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:7534502-Animals,
pubmed-meshheading:7534502-Carbohydrates,
pubmed-meshheading:7534502-DNA,
pubmed-meshheading:7534502-Energy Transfer,
pubmed-meshheading:7534502-Humans,
pubmed-meshheading:7534502-Lipids,
pubmed-meshheading:7534502-Proteins,
pubmed-meshheading:7534502-RNA,
pubmed-meshheading:7534502-Spectrometry, Fluorescence,
pubmed-meshheading:7534502-Virus Physiological Phenomena
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pubmed:year |
1995
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pubmed:articleTitle |
Fluorescence resonance energy transfer.
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pubmed:affiliation |
Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
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pubmed:publicationType |
Journal Article,
Review
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