"
Team:EPF Lausanne/Data
From 2014.igem.org
(Difference between revisions)
| Line 98: | Line 98: | ||
<div class="cntr"> | <div class="cntr"> | ||
| - | <u>Hypothesis:</u> Combining protein complementation techniques (split IFP1.4) to proteins going through dimerization (CpxR) upon activation due to a given stimuli (enveloppe stress) allows fast and specific spatiotemporal analysis of a stimuli | + | <u>Hypothesis:</u> Combining protein complementation techniques (split IFP1.4) to proteins going through dimerization (CpxR) upon activation due to a given stimuli (enveloppe stress) allows fast and specific spatiotemporal analysis of a stimuli. |
</div> | </div> | ||
| Line 107: | Line 107: | ||
<u>First intermediate objective:</u> explore if and how CpxR dimerizes in live E.Coli by analyzing the various orientations of CpxR - IFP1.4 fusions. | <u>First intermediate objective:</u> explore if and how CpxR dimerizes in live E.Coli by analyzing the various orientations of CpxR - IFP1.4 fusions. | ||
<br /><br /> | <br /><br /> | ||
| - | |||
| - | |||
<u>Second intermediate objective:</u> Analyse the temporal dynamics of the functional CpxR - IFP1.4 fusion protein by change of media. | <u>Second intermediate objective:</u> Analyse the temporal dynamics of the functional CpxR - IFP1.4 fusion protein by change of media. | ||
| Line 115: | Line 113: | ||
<u>Third intermediate objective:</u> Analyse the spatial dynamics of the functional CpxR - IFP1.4 fusion protein by microscopy. | <u>Third intermediate objective:</u> Analyse the spatial dynamics of the functional CpxR - IFP1.4 fusion protein by microscopy. | ||
</div> | </div> | ||
| + | |||
| + | |||
| + | The | ||
<!-- END ABSTRACT --> | <!-- END ABSTRACT --> | ||
Revision as of 23:15, 11 October 2014
DATA
Bacterial Biosensors
General Objective: Develop a fast and specific biosensor allowing spatiotemporal analysis of stimuli
To achieve the objective mentioned above, we put forward the following hypothesis:
Hypothesis: Combining protein complementation techniques (split IFP1.4) to proteins going through dimerization (CpxR) upon activation due to a given stimuli (enveloppe stress) allows fast and specific spatiotemporal analysis of a stimuli.
To validate this hypothesis we set ourselves three intermediate objectives:
First intermediate objective: explore if and how CpxR dimerizes in live E.Coli by analyzing the various orientations of CpxR - IFP1.4 fusions.
Second intermediate objective: Analyse the temporal dynamics of the functional CpxR - IFP1.4 fusion protein by change of media.
Third intermediate objective: Analyse the spatial dynamics of the functional CpxR - IFP1.4 fusion protein by microscopy.
Sponsors
Copyright © iGEM EPFL 2014. All Rights Reserved
