Difference between revisions of "Team:Kent/Description"
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| − | <li> Our Protein<br> | + | <li><font style="font-size:17px;font-weight:500;"> Our Protein</font><br> |
The protein that we have chosen to use is Sup35-NM derived from the Sup35 protein found in yeast. Amyloid formation occurs due to stacking interactions of the N domain and each individual Sup35-NM is sufficiently small and closely stacking as to allow the flow of electrons. The amyloid has desirable characteristics for nanostructures, such as heat resistance at both high and low temperatures ranging from 98℃ to -80℃, as well as high mechanical and chemical stability. </li> | The protein that we have chosen to use is Sup35-NM derived from the Sup35 protein found in yeast. Amyloid formation occurs due to stacking interactions of the N domain and each individual Sup35-NM is sufficiently small and closely stacking as to allow the flow of electrons. The amyloid has desirable characteristics for nanostructures, such as heat resistance at both high and low temperatures ranging from 98℃ to -80℃, as well as high mechanical and chemical stability. </li> | ||
| − | <li> Conduction <br> | + | <li> <font style="font-size:17px;font-weight:500;"> Conduction </font><br> |
To make our amyloid conductive we have the electron carrier cytochrome b562 bound to Sup35-NM as a fusion protein. Our protein follows the Sec export pathway. This means that our protein will be exported in an unfolded conformation. Type b cytochromes bind <i>haem</i> non-covalently and have four conserved histidine residues that bind to the central iron, thus allowing exogenous addition of <i>haem</i>. To allow electrons to pass to consecutive cytochromes the <i>haem</i> groups must be within 20 Angstroms of each other. </li> | To make our amyloid conductive we have the electron carrier cytochrome b562 bound to Sup35-NM as a fusion protein. Our protein follows the Sec export pathway. This means that our protein will be exported in an unfolded conformation. Type b cytochromes bind <i>haem</i> non-covalently and have four conserved histidine residues that bind to the central iron, thus allowing exogenous addition of <i>haem</i>. To allow electrons to pass to consecutive cytochromes the <i>haem</i> groups must be within 20 Angstroms of each other. </li> | ||
Revision as of 10:38, 2 September 2015
Project Description
Our project aims to produce self-assembling conductive nanowire by harnessing an endogenous amyloid export system in E.coli. This could be used to replace current nanowire technology which relies on chemical synthesis.
The protein that we have chosen to use is Sup35-NM derived from the Sup35 protein found in yeast. Amyloid formation occurs due to stacking interactions of the N domain and each individual Sup35-NM is sufficiently small and closely stacking as to allow the flow of electrons. The amyloid has desirable characteristics for nanostructures, such as heat resistance at both high and low temperatures ranging from 98℃ to -80℃, as well as high mechanical and chemical stability.
To make our amyloid conductive we have the electron carrier cytochrome b562 bound to Sup35-NM as a fusion protein. Our protein follows the Sec export pathway. This means that our protein will be exported in an unfolded conformation. Type b cytochromes bind haem non-covalently and have four conserved histidine residues that bind to the central iron, thus allowing exogenous addition of haem. To allow electrons to pass to consecutive cytochromes the haem groups must be within 20 Angstroms of each other.
Similar work has been carried out harnessing amyloid produced in vitro by a derivative of Sup35-NM with engineered cysteine residues to bind Nanogold particles. This work found that the distance between the Nanogold particles was too large to be conductive and thus a bridging technique was required to reduce of the 3-5nm gap, consequently forcing the diameter of the amyloid to be increased from 9-11nm to 80-200nm (Scheibel, 2003).
References
Scheibel, T., Parthasarathy, R., Sawicki, G., Lin, X. M., Jaeger, H., & Lindquist, S. L. (2003). Conducting nanowires built by controlled self-assembly of amyloid fibers and selective metal deposition. Proceedings of the National Academy of Sciences, 100(8), 4527-4532.
