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Full-Text Articles in Biochemistry
Investigation Of Potentially Catalytic Residues Of Uba5 Through Mutagenesis, Purification, And Structural Characterization, Grant Bradley
Investigation Of Potentially Catalytic Residues Of Uba5 Through Mutagenesis, Purification, And Structural Characterization, Grant Bradley
Senior Honors Projects, 2020-current
Ubiquitin-fold modifier 1 (Ufm1) is a member of the Ubiquitin (Ub) family of proteins whose primary function is degradation of proteins through a sequential mechanism of chemical reactions. Though Ufm1’s specific roles are largely unknown, this family of proteins has shown to play a part in a wide variety of processes, including regulation of the cell cycle1, secretory functions of cells2,3, and blood clotting4. Ufm1’s mechanism of action proceeds with the aid of three enzymes: an E1, E2, and E3. Uba5 is the E1 activating enzyme that is specific to Ufm1, and its mechanism of …
Studies Into The Structure And Function Of Various Domains Of Obscurin And Titin, Rachel A. Policke
Studies Into The Structure And Function Of Various Domains Of Obscurin And Titin, Rachel A. Policke
Senior Honors Projects, 2010-2019
Muscles give our bodies the ability to move by stretching and contracting. While contraction is accomplished by the well-known actin-myosin interaction, not much is known about stretch. Two integral muscle proteins involved in stretch are titin and obscurin; both are long rope-like protein molecules that seem to act as molecular springs. Mutations in these two proteins can lead to diseases such as hypertrophic cardiomyopathy and muscular dystrophy, as well as a variety of cancers. In an effort to understand muscle stretch and signaling on a more fundamental level, here we present the high resolution structure of obscurin Ig59, a domain …
Structural Elucidation Of Aggr-Activated Regulator, Aar, In Enteroaggregative Escherichia Coli, Andrew Heindel
Structural Elucidation Of Aggr-Activated Regulator, Aar, In Enteroaggregative Escherichia Coli, Andrew Heindel
Senior Honors Projects, 2010-2019
Travelers’ Diarrhea is the number one cause of childhood death in the world. Enteroaggregative Escherichia coli (EAEC) is one of the main causes of this disease. EAEC adhere to the surface of the intestine and stack in a brick-like pattern. Via an unstudied quorum-sensing mechanism, these bacteria express a variety of virulence factors that lead to diarrhea. The long-term goal of this research is to elucidate the mechanism by which EAEC changes from benign to virulent. A previously-unstudied open-reading frame in EAEC, AggR activated repressor (Aar), has recently been hypothesized to act as one of the major transcription factors influencing …