Event Title

C. elegan Muscle Mutations: How Small-Scale Changes Can Make a Big Impact

Location

Science Center, Bent Corridor

Start Date

10-28-2016 5:30 PM

End Date

10-28-2016 6:00 PM

Poster Number

25

Abstract

The general system of muscle movement has become increasingly well-known but there remains much about the cellular interactions before, during, and after the myosin powerstroke that are not fully understood. This study examines several different Caenorhabditis elegans myosin mutations and their effects on a worm’s muscle functions. Data was collected using a computer program that maps the worm’s swimming ability which provides different measures designed to give insight into the proper or improper functioning of the muscle. This study also analyzes the normal amino acid interactions and the effects of a mutation by examination of the crystal structure of myosin during pre-powerstroke, rigor, and post-rigor. By combining the data and crystal structure, this study shows that some of the mutations affected the muscle through changes in either force production or attachment of myosin cross bridges. This gives insight into how muscle movement is formed through energy going from chemical to mechanical energy. The information gathered can allow for a better understanding of the role of these amino acids and how small-scale changes in myosin can affect the functioning of the entire muscle.

Major

Biology

Project Mentor(s)

Taylor Allen, Biology

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Oct 28th, 5:30 PM Oct 28th, 6:00 PM

C. elegan Muscle Mutations: How Small-Scale Changes Can Make a Big Impact

Science Center, Bent Corridor

The general system of muscle movement has become increasingly well-known but there remains much about the cellular interactions before, during, and after the myosin powerstroke that are not fully understood. This study examines several different Caenorhabditis elegans myosin mutations and their effects on a worm’s muscle functions. Data was collected using a computer program that maps the worm’s swimming ability which provides different measures designed to give insight into the proper or improper functioning of the muscle. This study also analyzes the normal amino acid interactions and the effects of a mutation by examination of the crystal structure of myosin during pre-powerstroke, rigor, and post-rigor. By combining the data and crystal structure, this study shows that some of the mutations affected the muscle through changes in either force production or attachment of myosin cross bridges. This gives insight into how muscle movement is formed through energy going from chemical to mechanical energy. The information gathered can allow for a better understanding of the role of these amino acids and how small-scale changes in myosin can affect the functioning of the entire muscle.