Difference between revisions of "Part:BBa K2309024"

Latest revision as of 09:58, 1 November 2017

Reverse sequence of GF-17 for Lactococcus lactis

The linear cationic amphipathic peptide, GF-17, shows an important role in bacterial membrane permeation, but less toxic to human cells sheds new light on controlling invading pathogens. The reverse sequence of GF-17 is proved to have the similar function as GF-17. The structure of GF-17 reverse peptide dimer (VLNRLFDKIRQVIRKFG-VLNRLFDKIRQVIRKFG) is also α helical (Figure 4); (predicted by http://www.compbio.dundee.ac.uk/jpred/index.html). Although mechanisms of the swap of amino acids are not clear to us, we put the sequence anyway for further research.

Sequence and Features

Assembly Compatibility:

10
COMPATIBLE WITH RFC[10]
12
COMPATIBLE WITH RFC[12]
21
COMPATIBLE WITH RFC[21]
23
COMPATIBLE WITH RFC[23]
25
COMPATIBLE WITH RFC[25]
1000
COMPATIBLE WITH RFC[1000]

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 <partinfo>BBa_K2309024 short</partinfo>
-The linear cationic amphipathic peptide, GF-17, shows an important role in bacterial membrane permeation, but less toxic to human cells sheds new light on controlling invading pathogens. The reverse sequence of GF-17 is proved to have the similar function as GF-17. Although mechanisms of the swap of amino acids are not clear to us, we put the sequence anyway for further research.
+The linear cationic amphipathic peptide, GF-17, shows an important role in bacterial membrane permeation, but less toxic to human cells sheds new light on controlling invading pathogens. The reverse sequence of GF-17 is proved to have the similar function as GF-17.  The structure of GF-17 reverse peptide dimer (VLNRLFDKIRQVIRKFG-VLNRLFDKIRQVIRKFG) is also α helical (Figure 4); (predicted by http://www.compbio.dundee.ac.uk/jpred/index.html). Although mechanisms of the swap of amino acids are not clear to us, we put the sequence anyway for further research.
+https://static.igem.org/mediawiki/parts/f/fa/GF17R_prediction.png
 <!-- Add more about the biology of this part here