FINAL PROJECT: Abstract and Reader's Reponse > Using Photo-cross-linking to Discover New Binding Partners of Non-canonical Ubiquitin Chains
E, your reader might not need to understand the details of what you are talking about BUT more that your research can help us understand this protein. Why? Ubiquitin is part of these areas, all essential to medicine.
Apoptosis (cell death)
Cell division and multiplication
Degeneration of neurons and muscular cells
DNA transcription and repair
Immune and inflammatory response
Neural network morphogenesis
Organelle biogenesis
Processing of antigens
Receptor modulation
Ribosome biogenesis
Stress response pathway
Viral infection
--- perhaps you tell them this, instead, the applications argument.
Apoptosis (cell death)
Cell division and multiplication
Degeneration of neurons and muscular cells
DNA transcription and repair
Immune and inflammatory response
Neural network morphogenesis
Organelle biogenesis
Processing of antigens
Receptor modulation
Ribosome biogenesis
Stress response pathway
Viral infection
--- perhaps you tell them this, instead, the applications argument.
December 10, 2017 |
Marybeth Shea
Show them this Nobel Prize 2004 animation?
https://www.youtube.com/watch?v=jbc1QCu9hFg
https://www.youtube.com/watch?v=jbc1QCu9hFg
December 10, 2017 |
Marybeth Shea
Ubiquitin is a 76 amino acid protein that is found in all eukaryotic cells. In the cell, the protein functions as a molecular signal when attached to other proteins. Often, enzymes assemble chains of many ubiquitins into one ubiquitin chain through ubiquitin’s C-terminal glycine and one of ubiquitin’s 7 lysines. Based on the specific lysine that the ubiquitin chains formed upon, the ubiquitin chains has different functions. In the cell, ubiquitin chains exist that are linked through all 7 lysines. However, scientists only extensively understand the functions lysine 48-linked and lysine 63-linked ubiquitin chains. Ubiquitin chains linked through the 5 other lysines, called non-canonical chains, are less researched. The goal of this research is to discover more binding proteins to less researched non-canonical ubiquitin chains. If an unnatural photoreactive amino acid is incorporated into ubiquitin, then the photo-reactive ubiquitin can form a covalent attachment to any binding protein under certain light conditions. Currently, the accuracy of the photo-cross-linking process is being investigated. So far, photoreactive ubiquitin monomer, lysine 48-linked dimer, and lysine 63-linked dimer have been created. The photo-cross-linking ability of these proteins was tested with known binding proteins. After the preliminary testing, photoreactive non-canonical ubiquitin chains can be created and used to trap new binding proteins that cross-linked to them. The identification of new binding proteins to non-canonical ubiquitin chains opens up further investigations regarding the biological role of the interaction between the binding proteins and the non-canonical ubiquitin chains.
READER'S RESPONSE: So I understand that ubiquitin is a protein that exists in many cells, but I am still confused on its function and importance to the survival of the cell. I am still a bit confused about the chain creation process. How long can these chains be? How can a glycine and a lysine “link” together? Also, I do not understand what photo-cross-linking is and how a “photoreactive” amino acid can cause a protein to photo-cross-link. I thought that this abstract was very technical and complicated. In order for me to understand many of the biochemical aspects of the project, I need friendly figures and diagrams. I hope you provide these throughout the rest of the paper.