Difference between revisions of "Part:BBa K143038"
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<partinfo>BBa_K143038 short</partinfo> | <partinfo>BBa_K143038 short</partinfo> | ||
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− | <span class='h3bb'>Sequence and Features</span> | + | <span class='h3bb'><big>'''Sequence and Features'''</big></span> |
<partinfo>BBa_K143038 SequenceAndFeatures</partinfo> | <partinfo>BBa_K143038 SequenceAndFeatures</partinfo> | ||
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<partinfo>BBa_K143038 parameters</partinfo> | <partinfo>BBa_K143038 parameters</partinfo> | ||
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+ | ===Reference=== | ||
+ | <biblio> | ||
+ | #1 pmid=16061392 | ||
+ | #2 pmid=16997527 | ||
+ | #3 pmid=10974125 | ||
+ | </biblio> |
Revision as of 10:02, 18 September 2008
SacB-EAK16-II Fusion Protein
EAK16-II is a sixteen amino acid peptide that self-assembles to form β-sheet structures in an aqueous medium. The alternating positive and negative charges (--++--++) are responsible for creating an electrostatic attraction between adjacent peptides 1, triggering self-assembly when the EAK16-II peptides are exposed to physiological media or salt solution. When examined under SEM, a well-ordered nanofibre structure is formed by the association of the EAK16-II peptides and these nanofibres can futher aggregate to form a membranous 3D scaffold.
SacB is a signal peptide used in the Sec-SRP (secretory signal recognition particle) pathway by B. subtilis. Signal peptides are responsible for directing preproteins (secretory proteins with a signal peptide region attached) through an appropriate secretory pathway. In the case of the Sec-SRP signal peptide, they direct preproteins from the cytoplasm into the growth medium. SacB has been successfully used in the secretion of heterologous proteins such as acid-stable α-amylase, cystatin and interleukin-3 by B.subtilis 2.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
Reference
<biblio>
- 1 pmid=16061392
- 2 pmid=16997527
- 3 pmid=10974125
</biblio>