Linked Life Data

4590468

Source:http://linkedlifedata.com/resource/pubmed/id/4590468

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1974-3-31
pubmed:abstractText
Construction and characterization of double mutants altered in the structural gene of the tryptophan synthetase alpha chain of Escherichia coli revealed interactions between amino acid residues at positions 22 and 211. These interactions are specific for the particular amino acid residue at position 211. The results indicate also that amino acid residues which appear to be functionally near-equivalent in one configuration may strongly influence the activity of a protein with a subsequent change at another site. Seven independent suppressors of trpA218 (Leu22-Ser211) were isolated. Their properties suggest that all seven may suppress the codon (AGU/C) for Ser211. Six of the seven are co-transducible with glyV, the structural gene for the GGU/C-specific tRNA(Gly).
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0021-9193
pubmed:author
pubmed:issnType
Print
pubmed:volume
117
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
444-8
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1974
pubmed:articleTitle
Structural interactions between amino acid residues at positions 22 and 211 in the tryptophan synthetase alpha chain of Escherichia coli.
pubmed:publicationType
Journal Article