Difference between revisions of "Part:BBa K2729013"

Revision as of 01:14, 17 October 2018

DENV4 ancC-prM-E (Dengue Virus Serotype IV)

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.

Figure 1: Result of the Electrophoresis

As shown in Figure 1, the band of DENV4 prME come around 2,000 bp.

Sequence and Features

Assembly Compatibility:

10
INCOMPATIBLE WITH RFC[10]
Illegal EcoRI site found at 488
Illegal EcoRI site found at 1947
Illegal SpeI site found at 1219
12
INCOMPATIBLE WITH RFC[12]
Unknown
21
INCOMPATIBLE WITH RFC[21]
Unknown
23
INCOMPATIBLE WITH RFC[23]
Unknown
25
INCOMPATIBLE WITH RFC[25]
Illegal EcoRI site found at 488
Illegal EcoRI site found at 1947
Illegal SpeI site found at 1219
Illegal NgoMIV site found at 1207
1000
INCOMPATIBLE WITH RFC[1000]
Illegal SapI.rc site found at 793

Reference

- Membranotropic regions of the dengue virus prM protein

@@ Line 9: / Line 9: @@
 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 2018 EP (E,prME).png.png|thumb|left|300px| '''Figure 1:''' '''Result of the Electrophoresis''' ]]
+[[File:Tokyotech 2018 EP (E,prME).png|thumb|left|300px| '''Figure 1:''' '''Result of the Electrophoresis''' ]]
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