Template:Team:Bonn:NetworkData

content.text= "Regulating protein levels and conformation is a basic feature of any living organism, helping to maintain homeostasis and maximize efficiency while also increasing its versatility and adaptability. Thus, it is of great interest for basic research where tools are needed to provide protein regulation artificially. High spatiotemporal control is vital for essays which study protein function^{<a href='#1'>[1]</a>}, since often exact concentration or conformation is needed. In synthetic biology this is of particular importance since biochemical circuits rely on accurate mechanisms of control and oftentimes employ multiple means of induction.^{<a href='#2'>[2]</a>} However there is a multitude of methods available to induce changes in protein structure or expression.^{<a href='#1'>[1]</a><a href='#3'>[3]</a><a href='#4'>[4]</a><a href='#5'>[5]</a><a href='#6'>[6]</a>}Yet each technique has its own assets and drawbacks which are examined more closely in the following paragraphs.</br> </br> </br><table border="1"> <tr><td>Induction Method</td><td>Temporal resolution</td><td>Spatial Resolution</td><td>Reliability</td><td>Ease of use</td><td>Distinctive advantage</td></tr><tr><td>Light</td><td>Very high <µs</td><td>Very high</td><td>High</td><td>Cloning, genetical engineering required</td><td>Reversibel, in vivo</td></tr><tr><td>Chemical</td><td>Low 10sec - min</td><td>low</td><td>Very high (especially expression)</td><td>Very easy (expression), genetical engineering required (conformational)</td><td>Fine-tune gene expression</td></tr><tr><td>Heat</td><td>Low (expression only)</td><td>Very low (whole organism affected)</td><td>Very high</td><td>Very easy</td><td>Does not change protein conformation</td></tr><tr><td>Electrical</td><td>High <ms</td><td></td><td></td><td>Application can be difficult</td><td>Exact measurements</td></tr></table> <h2>References:</h2> <p><a name=1>1.</a> <a href='http://www.ncbi.nlm.nih.gov/pubmed/18272963'> Amy B Tyszkiewicz & Tom W Muir: <i>Activation of protein splicing with light in yeast.</i> &quot;Nature Methods&quot; | Vol.5 No.4 | 303 (April 2008)</a></p> <p><a name=2>2.</a> <a href='http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2955201'>X. Gu, M. Trybilo, S. Ramsay,M. Jensen, R. Fulton, S. Rosser, and D. Gilbert <i>Engineering a novel self-powering electrochemical biosensor.</i> &quot;Systems and Synthetic Biology&quot;4(3) (Sep 2010)</a></p> <p><a name=3>3.</a> <a href='http://www.ncbi.nlm.nih.gov/pubmed/?term=Heat-induced%20conformational%20change%20and%20increased%20chaperone%20activity%20of%20lens%20alpha-crystallin'> Das BK, Liang JJ, Chakrabarti B. <i>Heat-induced conformational change and increased chaperone activity of lens alpha-crystallin.</i> &quot;Current Eye Research&quot;  Apr;16(4):303-9  (1997)</a></p> <p><a name=4>4.</a> <a href='http://www.ncbi.nlm.nih.gov/pubmed/23359284'> Yang J, Yang H, Sun X, Delaloye K, Yang X, Moller A, Shi J, Cui J. <i>Interaction between residues in the Mg2+-binding site regulates BK channel activation.</i> &quot;The journal of general physiology&quot; (Feb 2013)</a></p> <p><a name=5>5.</a> <a href='http://www.ncbi.nlm.nih.gov/pubmed/10537212> Richard DJ, Sawers G, Sargent F, McWalter L, Boxer DH. <i>Transcriptional regulation in response to oxygen and nitrate of the operons encoding the [NiFe] hydrogenases 1 and 2 of Escherichia coli.</i> &quot;Microbiology&quot;145 ( Pt 10)  (Oct 1999)</a></p> <p><a name=6>6.</a> <a href='http://www.ncbi.nlm.nih.gov/pmc/articles/PMC97448/'> Maen Qa&quot;Dan, Lea M. Spyres, and Jimmy D. Ballard <i>pH-Induced Conformational Changes in Clostridium difficile Toxin B.</i> &quot;Infection and Immunity&quot; 68(5) (May 2000)</a></p>";