Proc. Natl. Acad. Sci. U.S.A.

We present an approach that allows rapid determination of the topology of Escherichia coli inner-membrane proteins by a combination of topology prediction and limited fusion-protein analysis. We derive new topology models for 12 inner-membrane proteins: MarC, PstA, TatC, YaeL, YcbM, YddQ, YdgE, YedZ, YgjV, YiaB, YigG, and YnfA. We estimate that our approach should make it possible to arrive at highly reliable topology models for roughly 10% of the approximately 800 inner-membrane proteins thought to exist in E. coli.

Source:http://purl.uniprot.org/citations/11867724

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We present an approach that allows rapid determination of the topology of Escherichia coli inner-membrane proteins by a combination of topology prediction and limited fusion-protein analysis. We derive new topology models for 12 inner-membrane proteins: MarC, PstA, TatC, YaeL, YcbM, YddQ, YdgE, YedZ, YgjV, YiaB, YigG, and YnfA. We estimate that our approach should make it possible to arrive at highly reliable topology models for roughly 10% of the approximately 800 inner-membrane proteins thought to exist in E. coli.
skos:exactMatch
uniprot:name
Proc. Natl. Acad. Sci. U.S.A.
uniprot:author
Chin C.-N., Drew D., Nilsson J., Sjoestrand D., Urbig T., de Gier J.-W., von Heijne G.
uniprot:date
2002
uniprot:pages
2690-2695
uniprot:title
Rapid topology mapping of Escherichia coli inner-membrane proteins by prediction and PhoA/GFP fusion analysis.
uniprot:volume
99
dc-term:identifier
doi:10.1073/pnas.052018199