Characterization of Cardiac Troponin C FRET Constructs to Analyze Structural Changes Induced by Divalent Cation Binding
This research focuses on the characterization of three isoforms of the human cardiac Troponin C protein previously designed and created by Myriam Badr. These isoforms differ both in the fluorophores bound to the N and C termini and the size of the linker sequences between the...
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| Format: | Others |
| Language: | English English |
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Florida State University
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| Online Access: | http://purl.flvc.org/fsu/fd/FSU_2016SP_Lentsch_fsu_0071N_13055 |
| Summary: | This research focuses on the characterization of three isoforms of the human cardiac Troponin C protein previously designed and
created by Myriam Badr. These isoforms differ both in the fluorophores bound to the N and C termini and the size of the linker sequences
between the fluorophores and TnC protein. Troponin C is notable for its function in Ca2+ binding, which, in functioning muscle, induces a
conformational change. This reveals the hidden myosin head binding site and allows contraction to proceed. Using fluorometer analysis to
measure changes in FRET, the structural changes each undergoes in the presence of calcium, magnesium, and calcium in the presence of
magnesium were analyzed to better understand the functioning of each of these proteins under physiological conditions. Since deficits in
cardiac troponin C function have been implicated in some cases of familial hypertrophic cardiomyopathy, it is important to better
understand how function changes with the size and shape of the cardiac troponin C protein. With this in mind, we hope to gain a more
complete understanding of human cardiac troponin C function. === A Thesis submitted to the Department of Biological Science in partial fulfillment of the Master of
Science. === Spring Semester 2016. === February 19, 2016. === cardiac, FRET, troponin === Includes bibliographical references. === P. Bryant Chase, Professor Co-Directing Thesis; Jose R. Pinto, Professor Co-Directing Thesis;
George Bates, Committee Member; Michael Meredith, Committee Member. |
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