Submission Date
7-23-2015
Document Type
Paper- Restricted to Campus Access
Department
Chemistry
Faculty Mentor
Amanda Reig
Project Description
How a protein’s structure will determine its function is not very well understood. One way we study this relationship is by using a de novo model protein because they represent a simplified version of the protein and are easy to mutate and synthesize in a lab. We are focused on studying the class of binuclear non-heme di-iron enzymes because these proteins are all very similar in structure but carry out different functions. I am working on creating a model for myo-inositol oxygenase (MIOX) which plays a role in glycol oxygenation. To see how mutations will affect the function, metal binding assays with iron and cobalt were performed, as well as reactivity assays to observe the oxidase and oxygenase properties.
Recommended Citation
Philip, Christine M., "Characterization of 4-Histidine/2-Carboxylate Di-Iron De Novo Proteins" (2015). Chemistry Summer Fellows. 2.
https://digitalcommons.ursinus.edu/chem_sum/2
Restricted
Available to Ursinus community only.
Comments
Presented during the 17th Annual Summer Fellows Symposium, July 24, 2015 at Ursinus College.
Supported by a National Institutes of Health Academic Research Enhancement Award (AREA) grant (R15-GM110657).