Difference between revisions of "Part:BBa K2262001"
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+ | McManus, A.M.; Nielsen, K.J.; Marcus, J.P.; Harrison, S.J.; Green, J.L.; Manners, J.M.; Craik, D.J. "MiAMP1, a novel protein from Macadamia integrifolia adopts a Greek key beta-barrel fold unique amongst plant antimicrobial proteins." J. Mol. Biol. 1999, 293, 629-638 | ||
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Revision as of 19:44, 29 October 2017
T7 Promoter+RBS+MiAMP1
Introduction:
This peptide is from the MiAMP family. It is an anti-fungal peptide which inhibits the growth of a variety of fungi and has no activity against E.coli. The mechanism of the peptide is to bind specifically to beta-(1,3)-glucans in fungal cell walls through conserved polar and aromatic residues. NCTU_Formosa used it to be one of a training data for creating our anti-fungal peptide scoring card.
Reference:
McManus, A.M.; Nielsen, K.J.; Marcus, J.P.; Harrison, S.J.; Green, J.L.; Manners, J.M.; Craik, D.J. "MiAMP1, a novel protein from Macadamia integrifolia adopts a Greek key beta-barrel fold unique amongst plant antimicrobial proteins." J. Mol. Biol. 1999, 293, 629-638
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]