Switch to
Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
|
pubmed:dateCreated |
1990-6-12
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pubmed:abstractText |
C-terminally deleted analogs of human interleukin-6 (IL-6) have been constructed at the cDNA level, and after cell-free transcription and translation their biological activity was analyzed. Removal of only 4 amino acids resulted in complete loss of biological activity as determined by the B9 cell proliferation assay. Secondary structure prediction of human IL-6 resulted in 58% helix, 14% beta-structure, and 28% turn and coil (average of 3 independent methods). The circular dichroism of recombinant human IL-6 was measured in the near and far UV. Evaluation of the latter in terms of secondary structures gave 67% helix, 15% beta-structure, and 18% turn and coil.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Mar
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pubmed:issn |
0014-5793
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pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
26
|
pubmed:volume |
262
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
323-6
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:2335213-Animals,
pubmed-meshheading:2335213-Cell Line,
pubmed-meshheading:2335213-Circular Dichroism,
pubmed-meshheading:2335213-DNA,
pubmed-meshheading:2335213-Humans,
pubmed-meshheading:2335213-Interleukin-6,
pubmed-meshheading:2335213-Mutation,
pubmed-meshheading:2335213-Protein Biosynthesis,
pubmed-meshheading:2335213-Protein Conformation,
pubmed-meshheading:2335213-Rats,
pubmed-meshheading:2335213-Structure-Activity Relationship,
pubmed-meshheading:2335213-Transcription, Genetic
|
pubmed:year |
1990
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pubmed:articleTitle |
Structure-function analysis of human interleukin-6. Evidence for the involvement of the carboxy-terminus in function.
|
pubmed:affiliation |
Institut für Biochemie der RWTH Aachen, FRG.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|