Difference between revisions of "Part:BBa K2729012"
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The prM protein consists of an N-terminal pr domain followed by the M protein separated by a furin cleavage site.(15) The pr part of the protein consists mainly of β-strands, whereas the M portion consists of a linear structure followed by a mainly α-helical stem region and two transmembrane helices. | The prM protein consists of an N-terminal pr domain followed by the M protein separated by a furin cleavage site.(15) The pr part of the protein consists mainly of β-strands, whereas the M portion consists of a linear structure followed by a mainly α-helical stem region and two transmembrane helices. | ||
| − | [[File:Tokyotech | + | [[File:Tokyotech 2018 EP (E,prME).png|thumb|left|300px| '''Figure 1:''' '''Result of the Electrophoresis''' ]] |
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Revision as of 01:14, 17 October 2018
DENV3 ancC-prM-E (Dengue Virus Serotype III)
Usage and Biology
Flavivirus Capsid (C), prM (precursor Membrane) and Envelope (E) are structural proteins responsible for gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle.
Characterization
The prM protein consists of an N-terminal pr domain followed by the M protein separated by a furin cleavage site.(15) The pr part of the protein consists mainly of β-strands, whereas the M portion consists of a linear structure followed by a mainly α-helical stem region and two transmembrane helices.
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As shown in Figure 1, the band of DENV3 prME come around 2,0000bp.
Sequence and Features
Assembly Compatibility:
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]