Difference between revisions of "Part:BBa K2729012"
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==Characterization== | ==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. | 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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| + | [[File:Tokyotech electrophoresis あはは.png|thumb|left|300px| '''Figure 1:''' '''Result of the Electrophoresis''' ]] | ||
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| + | <br> | ||
| + | As shown in Figure 1, the band of DENV3 prME come around 2,0000bp. | ||
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==Sequence and Features== | ==Sequence and Features== | ||
Revision as of 18:25, 16 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.
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]