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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
5
|
| pubmed:dateCreated |
1989-3-16
|
| pubmed:abstractText |
The 500 MHz 1H-NMR spectra of dimeric protein L12 from ribosomes shows a limited number of unusually sharp signals at room temperature. This is interpreted as evidence for substantial segmental flexibility of the region in the protein molecule. We have analysed the extent of the flexible region and also the size of the organized structures of the molecule. Thus residues 37-50 were found to be highly mobile whereas the N-terminal and C-terminal region are organized into folded domains.
|
| pubmed:language |
rus
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:issn |
0026-8984
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
22
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
1359-70
|
| pubmed:dateRevised |
2009-11-19
|
| pubmed:meshHeading |
pubmed-meshheading:3065618-Amino Acid Sequence,
pubmed-meshheading:3065618-Bacterial Proteins,
pubmed-meshheading:3065618-Escherichia coli,
pubmed-meshheading:3065618-Geobacillus stearothermophilus,
pubmed-meshheading:3065618-Magnetic Resonance Spectroscopy,
pubmed-meshheading:3065618-Protein Conformation,
pubmed-meshheading:3065618-Ribosomal Proteins
|
| pubmed:articleTitle |
[1H-NMR study of protein L7/L12 from bacterial ribosomes].
|
| pubmed:publicationType |
Journal Article,
English Abstract
|