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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1995-4-11
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pubmed:abstractText |
The molecular architecture of native GroEL has been studied by solution X-ray scattering. The radius of gyration for the native molecule was estimated to be 66.0 A in 50 mM Tris-HCl, 100 mM KCl at pH 7.5 and 25 degrees C. The maximum dimension was estimated to be 170 A, based on the pair distance distribution function. A cylindrical structure or two heptameric rings was found to be the best for native GroEL among structures examined by using a multi-sphere model analysis in which the radius of constituent sphere was 6 A. The results of the model analysis show that the radius of GroEL is 68.0 A and the height is 150.7 A. Unexpectedly, the central penetrating hole through GroEL was not confirmed in the best-fit structure.
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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 |
0301-4622
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
53
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
259-66
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:7880961-Chaperonin 60,
pubmed-meshheading:7880961-Escherichia coli,
pubmed-meshheading:7880961-Models, Chemical,
pubmed-meshheading:7880961-Protein Conformation,
pubmed-meshheading:7880961-Scattering, Radiation,
pubmed-meshheading:7880961-Solutions,
pubmed-meshheading:7880961-X-Rays
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pubmed:year |
1995
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pubmed:articleTitle |
Solution X-ray scattering study on the chaperonin GroEL from Escherichia coli.
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pubmed:affiliation |
Department of Biochemistry, Dokkyo University School of Medicine, Tochigi, Japan.
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pubmed:publicationType |
Journal Article
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