AuthorBowman, Nicholas Spencer
MetadataShow full item record
PublisherThe University of Arizona.
RightsCopyright © is held by the author. Digital access to this material is made possible by the University Libraries, University of Arizona. Further transmission, reproduction or presentation (such as public display or performance) of protected items is prohibited except with permission of the author.
AbstractFUS is an RNA binding protein that facilitates the process of transcription. When mutated, it is known to cause ALS, a degenerative neurological disease. Labeling this protein can be done by the use of a TBD molecule which binds FUS at Tyr residues in its low complexity domain. In wild type FUS, Tyr residues are abundant and available for labeling. In mutated FUS, the protein forms aggregates, cutting off the Tyr availability. These means a difference in labeling can be quantified and used to diagnose those with ALS. Temperature affects the kinetics of the labeling in a variety of ways. The temperature that yields the most intense bands and clearest labeling was determined by these experiments. With the given data, the temperatures of most interest are 4, 35, and 45 degrees Celsius.
Degree ProgramHonors College
Biochemistry and Molecular Biophysics