Source:http://linkedlifedata.com/resource/pubmed/id/16852567
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
26
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pubmed:dateCreated |
2006-7-20
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pubmed:abstractText |
We used single-pair fluorescence resonance energy transfer (spFRET) to track distance changes between domains of fluorescently labeled calmodulin (CaM) on the sub-millisecond time scale. In most cases, CaM remained in the same conformational substate over time periods of up to 1 ms, showing that conformational interchange occurs on a longer time scale. However, in some instances, apparent transitions between conformational substates could be detected. The magnitude of sub-millisecond motion within the dominant conformational substate also revealed fluctuations in distance between domains that were dependent on pH and ionic strength.
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pubmed:grant | |
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 |
Jul
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pubmed:issn |
1520-6106
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
7
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pubmed:volume |
109
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
12658-62
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pubmed:dateRevised |
2007-12-3
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pubmed:meshHeading |
pubmed-meshheading:16852567-Animals,
pubmed-meshheading:16852567-Calmodulin,
pubmed-meshheading:16852567-Diffusion,
pubmed-meshheading:16852567-Fluorescence Resonance Energy Transfer,
pubmed-meshheading:16852567-Humans,
pubmed-meshheading:16852567-Models, Molecular,
pubmed-meshheading:16852567-Motion,
pubmed-meshheading:16852567-Protein Structure, Tertiary,
pubmed-meshheading:16852567-Thermodynamics
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pubmed:year |
2005
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pubmed:articleTitle |
Single-molecule tracking of sub-millisecond domain motion in calmodulin.
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pubmed:publicationType |
Letter,
Research Support, N.I.H., Extramural
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