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Engineered Switch Protein Inspired By Novel Protein Affinity Transition Mode, Liang Fang
Engineered Switch Protein Inspired By Novel Protein Affinity Transition Mode, Liang Fang
Doctoral Dissertations
Many natural proteins involved in complex biological processes such as ligand binding and protein folding demonstrate multiple, allosterically-regulated conformational states, with protein activity regulated by effector molecules. The alpha L integrin and its inserted domain (I domain) is one example of such a protein. The binding of the effector molecule such as talin or filamin to the cytoplasmic domain of the integrin increases the binding affinity between I- domain and its ligand intercellular adhesion molecule-1, known as ICAM-1.There are multiple models attempting to describe the mechanism responsible for the change in binding affinity. According to research conducted by our lab, …
A Tale Of Two Protein Switches: Engineering, Characterizing, And Understanding A Novel And A Natural Switch, James Vincent Price
A Tale Of Two Protein Switches: Engineering, Characterizing, And Understanding A Novel And A Natural Switch, James Vincent Price
Doctoral Dissertations
Throughout nature, many proteins provide a specific function in response to some input signal (e.g., phosyphorylation, pH, etc.), a process that is oftentimes described as switching a protein “on” or “off.” The advent of protein engineering has allowed for the creation and understanding of chimeric proteins for uses in a number of applications such as therapeutics, biosensors and energy production. Two proteins, hemagglutinin (HA) of fowl plague influenza virus and a chimeric protein comprising a fusion between the LFA-1 I domain and the EF3 and EF4 hands of calmodulin, have been investigated in this dissertation. Both of these proteins undergo …