Difference between revisions of "Team:Aachen/Description"
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<p align="justify" style="padding-left:1.0cm; padding-right:1.0cm; font-size: 16px;"><i>Escherichia coli</i> is widely used in synthetic biology. It offers the advantage of being a comparatively simple and well-understood model organism while being easy to handle in the laboratory environment. Also, an expansion of the genetic code has already been successfully implemented in <i>E. coli</i> multiple times [1]–[4] by introducing an orthogonal tRNA/aminoacyl-synthetase pair.<br/> | <p align="justify" style="padding-left:1.0cm; padding-right:1.0cm; font-size: 16px;"><i>Escherichia coli</i> is widely used in synthetic biology. It offers the advantage of being a comparatively simple and well-understood model organism while being easy to handle in the laboratory environment. Also, an expansion of the genetic code has already been successfully implemented in <i>E. coli</i> multiple times [1]–[4] by introducing an orthogonal tRNA/aminoacyl-synthetase pair.<br/> | ||
| − | Therefore, working in <i>E. coli</i> is an obvious choice.<br/> | + | Therefore, working in <i>E. coli</i> is an obvious choice.<br/><br/> |
Due to a limited range of tRNA/aminoacyl-synthetase pairs for non-canonical amino acids in general and especially for those that act orthogonally in <i>E. coli</i>, photocaging serine in the active site of subtilisin E with DMNB-serine is currently not possible. Hence, another strategy is needed to produce temporarily inactive proteases. This part of the project focuses on utilizing the maturation process of subtilisin E.<br/> | Due to a limited range of tRNA/aminoacyl-synthetase pairs for non-canonical amino acids in general and especially for those that act orthogonally in <i>E. coli</i>, photocaging serine in the active site of subtilisin E with DMNB-serine is currently not possible. Hence, another strategy is needed to produce temporarily inactive proteases. This part of the project focuses on utilizing the maturation process of subtilisin E.<br/> | ||
Revision as of 09:48, 13 October 2016
Project Description
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Escherichia coli is widely used in synthetic biology. It offers the advantage of being a comparatively simple and well-understood model organism while being easy to handle in the laboratory environment. Also, an expansion of the genetic code has already been successfully implemented in E. coli multiple times [1]–[4] by introducing an orthogonal tRNA/aminoacyl-synthetase pair.
Therefore, working in E. coli is an obvious choice.
Due to a limited range of tRNA/aminoacyl-synthetase pairs for non-canonical amino acids in general and especially for those that act orthogonally in E. coli, photocaging serine in the active site of subtilisin E with DMNB-serine is currently not possible. Hence, another strategy is needed to produce temporarily inactive proteases. This part of the project focuses on utilizing the maturation process of subtilisin E.
