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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
|
pubmed:dateCreated |
1998-8-11
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pubmed:abstractText |
Models of the bacterial ribosome based on recent structural analyses are beginning to provide new insights into the protein synthetic machinery. Central to evolving models are the high-resolution structures of individual ribosomal proteins, which represent detailed probes of their local RNA and protein environments. Ribosomal proteins are extremely ancient molecules; the structures therefore also provide a unique window into early protein evolution. Many of the proteins contain domains that are present in more recently evolved families of RNA- and DNA-binding proteins. Such structural homology can be used to predict mechanisms by which proteins interact with RNA in the ribosome.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Jun
|
pubmed:issn |
0968-0004
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
23
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
208-12
|
pubmed:dateRevised |
2005-11-16
|
pubmed:meshHeading | |
pubmed:year |
1998
|
pubmed:articleTitle |
Ribosomal protein structures: insights into the architecture, machinery and evolution of the ribosome.
|
pubmed:affiliation |
Dept of Biochemistry, University of Utah School of Medicine, Salt Lake City 84132, USA.
|
pubmed:publicationType |
Journal Article,
Review
|