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.
Recommended Citation
LaTourrette, Katherine, "C. elegan Muscle Mutations: How Small-Scale Changes Can Make a Big Impact" (2016). Celebration of Undergraduate Research. 38.
https://digitalcommons.oberlin.edu/cour/2016/posters/38
Major
Biology
Project Mentor(s)
Taylor Allen, Biology
Document Type
Poster
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.