Difference between revisions of "Team:British Columbia/Human Practices"
m |
m |
||
| Line 98: | Line 98: | ||
<div class="col-sm-9" style="padding-left: 25px"> | <div class="col-sm-9" style="padding-left: 25px"> | ||
<section id="who-we-are" class="anchor"> | <section id="who-we-are" class="anchor"> | ||
| − | <h3 style="top: | + | <h3 style="maring-top: 0">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 | ||
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 | 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 | ||
Revision as of 22:34, 16 October 2016
Human Practices
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
