Preferred Name - First Author
Date of Award
Bachelor of Science (BS)
Department of Chemistry and Biochemistry
Nathan T. Wright
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.
Caldwell, Tracy A., "Examination of the Structure, Force Resistance, and Elasticity of Muscle Proteins" (2015). Senior Honors Projects, 2010-current. 110.