Senior Honors Projects, 2010-2019
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Date of Graduation
Spring 2015
Document Type
Thesis
Degree Name
Bachelor of Science (BS)
Department
Department of Chemistry and Biochemistry
Advisor(s)
Nathan T. Wright
Abstract
Obscurin and titin are made up of independently folded domains that can be studied individually. Both are comprised of mostly Ig (immunoglobulin) or FnIII (Fibronectin type III)- like domains, which are made of two beta sheets held together by a hydrophobic core. High resolution structures of a limited number of both titin and obscurin domains have been determined using both nuclear magnetic resonance (NMR) and X-ray crystallography. These structures have been complemented by low resolution methods such as small angle X-ray scattering (SAXS) and cryo-electron microscopy (cryo-EM). Here, other high and low resolution structures not previously published will be presented in order to investigate how their response to force, elasticity, flexibility, and orientation of domains aids in their function.
Recommended Citation
Caldwell, Tracy A., "Examination of the structure, force resistance, and elasticity of muscle proteins" (2015). Senior Honors Projects, 2010-2019. 110.
https://commons.lib.jmu.edu/honors201019/110
