Senior Honors Projects, 2010-current

Preferred Name - First Author

Policke, Rachel

Date of Award

Spring 2017

Document Type

Thesis

Degree Name

Bachelor of Science (BS)

Department

Department of Chemistry and Biochemistry

Advisor(s)

Nathan T. Wright

Abstract

Muscles give our bodies the ability to move by stretching and contracting. While contraction is accomplished by the well-known actin-myosin interaction, not much is known about stretch. Two integral muscle proteins involved in stretch are titin and obscurin; both are long rope-like protein molecules that seem to act as molecular springs. Mutations in these two proteins can lead to diseases such as hypertrophic cardiomyopathy and muscular dystrophy, as well as a variety of cancers. In an effort to understand muscle stretch and signaling on a more fundamental level, here we present the high resolution structure of obscurin Ig59, a domain involved in titin/obscurin binding. We also describe how unbound titin moves when stretched. Last, we describe ongoing work in elucidating the high-resolution structures and activation/inhibition mechanisms of obscurin domains Rho-GEF, Rho-GEF-PH, kinase I (KI), and kinase II (KII).

Included in

Biochemistry Commons

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