Difference between revisions of "Team:British Columbia/Human Practices"

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         <ul class="nav sidebar-nav nav-pills nav-stacked">
 
         <ul class="nav sidebar-nav nav-pills nav-stacked">
 
           <li class="active"><a href="#who-we-are">Who We Are</a></li>
 
           <li class="active"><a href="#who-we-are">Who We Are</a></li>
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           <li><a href="#background">S-layer Engineering</a></li>
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           <li><a href="#background">Background</a></li>
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           <li><a href="#bio-pathways">Biosynthetic Pathways</a></li>
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           <li><a href="#sci-comm">Science Communication</a></li>
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          <li><a href="#consortia">Consortia</a></li>
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           <h3>S-layer Engineering</h3>
 
           <h3>S-layer Engineering</h3>
 
           <p style="text-align: left; height: 600px">The mesophilic organism Lysinibacillus sphaericus CCM 2177 produces the surface (S)-layer protein SbpA, which after secretion completely covers the cell surface with a crystalline array exhibiting square lattice symmetry. Because of its excellent
 
           <p style="text-align: left; height: 600px">The mesophilic organism Lysinibacillus sphaericus CCM 2177 produces the surface (S)-layer protein SbpA, which after secretion completely covers the cell surface with a crystalline array exhibiting square lattice symmetry. Because of its excellent
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         <section id="bio-pathways" class="anchor" style="height: 600px">
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         <section id="background" class="anchor" style="height: 600px">
 
           <h3>Biosynthetic Pathways</h3>
 
           <h3>Biosynthetic Pathways</h3>
 
         </section>
 
         </section>
  
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         <section id="consortia" class="anchor" style="height: 600px">
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         <section id="sci-comm" class="anchor" style="height: 600px">
 
           <h3>Consortia</h3>
 
           <h3>Consortia</h3>
 
         </section>
 
         </section>

Revision as of 21:48, 16 October 2016

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Human Practices

Human Practices

Overview

S-layer Engineering

The mesophilic organism Lysinibacillus sphaericus CCM 2177 produces the surface (S)-layer protein SbpA, which after secretion completely covers the cell surface with a crystalline array exhibiting square lattice symmetry. Because of its excellent in vitro recrystallization properties on solid supports, SbpA represents a suitable candidate for genetically engineering to create a versatile self-assembly system for the development of a molecular construction kit for nanobiotechnological applications. The first goal of this study was to investigate the surface location of 3 different C-terminal amino acid positions within the S-layer lattice formed by SbpA. Therefore, three derivatives of SbpA were constructed, in

Biosynthetic Pathways

Consortia