rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1992-4-3
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pubmed:abstractText |
Circular dichroism was used to study the secondary structure of protein kinase C (PKC) in aqueous solution and the conformational changes resulting due to the presence of its regulatory cofactors (e.g. Ca2+, phosphatidylserine (PS) and phorbol 12-myristate 13-acetate (PMA)). Computer analysis of the CD data for the estimates of secondary structure showed that PKC maintains a highly ordered structure containing 36% alpha-helix, 57% beta-sheet and 7% beta-turn. PKC displays a minor conformational change upon addition of Ca2+. However, a larger change is observed on adding phosphatidylserine vesicles in the presence of Ca2+. In this case, the alpha-helix content is decreased by approx. 35% and beta-sheet increased by approx. 16%. The protein does not experience further significant changes in conformation on adding PMA.
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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 |
Feb
|
pubmed:issn |
0006-3002
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pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
13
|
pubmed:volume |
1119
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
19-26
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:1540630-Adenosine Triphosphate,
pubmed-meshheading:1540630-Animals,
pubmed-meshheading:1540630-Binding Sites,
pubmed-meshheading:1540630-Brain,
pubmed-meshheading:1540630-Calcium,
pubmed-meshheading:1540630-Cattle,
pubmed-meshheading:1540630-Circular Dichroism,
pubmed-meshheading:1540630-Liposomes,
pubmed-meshheading:1540630-Mathematics,
pubmed-meshheading:1540630-Molecular Weight,
pubmed-meshheading:1540630-Phosphatidylserines,
pubmed-meshheading:1540630-Protein Binding,
pubmed-meshheading:1540630-Protein Conformation,
pubmed-meshheading:1540630-Protein Kinase C,
pubmed-meshheading:1540630-Tetradecanoylphorbol Acetate
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pubmed:year |
1992
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pubmed:articleTitle |
Circular dichroic studies of protein kinase C and its interactions with calcium and lipid vesicles.
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pubmed:affiliation |
Department of Biophysics, Boston University School of Medicine, Housman Medical Research Center, MA 02118.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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