Difference between revisions of "Part:BBa K143038"

 
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<partinfo>BBa_K143038 short</partinfo>
 
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EAK16-II is a sixteen amino acid peptide that self-assembles to form &#946;-sheet structures in an aqueous medium. The alternating positive and negative charges (--++--++) are responsible for creating an electrostatic attraction between adjacent peptides <cite>1</cite>, 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.
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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 &#945;-amylase, cystatin and interleukin-3 by B.subtilis <cite>2</cite>.
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EAK16-II is a sixteen amino acid peptide that self-assembles to form &#946;-sheet structures in an aqueous medium. The alternating positive and negative charges (--++--++) are responsible for creating an electrostatic attraction between adjacent peptides <cite>1</cite>, 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.
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<br>
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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 &#945;-amylase, cystatin and interleukin-3 by ''B. subtilis'' <cite>2</cite>.
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<span class='h3bb'>Sequence and Features</span>
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<span class='h3bb'><big>'''Sequence and Features'''</big></span>
 
<partinfo>BBa_K143038 SequenceAndFeatures</partinfo>
 
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<partinfo>BBa_K143038 parameters</partinfo>
 
<partinfo>BBa_K143038 parameters</partinfo>
 
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===Reference===
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<biblio>
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#1 pmid=16061392
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#2 pmid=16997527
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</biblio>

Latest revision as of 13:13, 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


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]


Reference

<biblio>

  1. 1 pmid=16061392
  2. 2 pmid=16997527

</biblio>