DNA Origami Assembly for the Tar Chemoreceptor

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== Introduction to Chemotaxis ==
== Introduction to Chemotaxis ==
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Chemotaxis is the process by which bacteria sense chemicals in their environment. This is done through the use of chemoreceptors to sense a chemical gradient that they can follow towards higher concentrations of food or away from higher concentrations of poisons or other unfavorable conditions. The Tar chemoreceptor is involved with the sensing of aspartate, a common amino acid, by binding aspartate in the extracellular portion of the protein and then propagates a signal down the receptor to activate a pathway to alter movement. [Add picture of chemoreceptor here? Are there any that are open source?]
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Chemotaxis is the process by which bacteria sense chemicals in their environment. This is done through the use of chemoreceptors to sense a chemical gradient that they can follow towards higher concentrations of food or away from higher concentrations of poisons or other unfavorable conditions. The Tar chemoreceptor is involved with the sensing of aspartate, a common amino acid, by binding aspartate in the extracellular portion of the protein and then propagates a signal down the receptor to activate a pathway to alter movement. '''[Add picture of chemoreceptor here? Are there any that are open source?]'''
== Possible Applications of Chemotaxis ==
== Possible Applications of Chemotaxis ==
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==Attachment to DNA==
==Attachment to DNA==
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The protein receptor dimer is attached to the DNA tetrahedron using NTA-functionalized DNA. This means that the DNA has an NTA, or nitrilotriaceticacid, is able to coordinate with nickel ions, shown in green, which is also able to coordinate with histidines. The Tar chemoreceptor has six histidines added to the N-terminus of the protein ''in vitro'', which should be able to coordinate with the nickel ion as well, creating a coordination complex.
== Structural highlights ==
== Structural highlights ==

Revision as of 03:40, 31 October 2018

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References

  1. Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
  2. Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644

Proteopedia Page Contributors and Editors (what is this?)

Dominique Kiki Carey, Michal Harel

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