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PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1993-6-11
pubmed:abstractText
Multiple copies of the Johnsongrass mosaic virus coat protein synthesized in Escherichia coli can readily assemble to form potyvirus-like particles. This E. coli expression system has been used to identify some of the key amino acid residues, within the core region of the coat protein, required for assembly. The two charged residues R194 and D238 previously proposed theoretically to be involved as a pair in the construction of a salt bridge crucial for the assembly process were targeted for site-directed mutagenesis. The results from our experiments suggest that the two residues are required for the assembly process but are not necessarily involved as a pair in a common salt bridge.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0022-1317
pubmed:author
pubmed:issnType
Print
pubmed:volume
74 ( Pt 5)
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
893-6
pubmed:dateRevised
2000-12-18
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Site-directed mutagenesis of a potyvirus coat protein and its assembly in Escherichia coli.
pubmed:affiliation
CSIRO, Division of Biomolecular Engineering, Parkville Laboratory, Victoria, Australia.
pubmed:publicationType
Journal Article