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Metea Valley High School ESRP 2021

Effect of Titin on Lattice Spacing in Sarcomere Structure

Authors:

  • Students:
    • Jonathan Barker
    • Sahaja Danthurthy
    • Hariharan Kannan
    • Anish Khot
    • Ayush Khot
    • Sannidhi Mohan
    • Pravallika Padyala
    • Zachary White
  • Teachers:
    • Vanessa Troiani
  • Mentors:
    • Thomas Irving (Illinois Institute of Technology, Advanced Photon Source, Biophysics Collaborative Access Team)

Advanced Photon Source Sector 18: BioCAT

When muscle contraction was first researched and studied, it was thought that thick and thin filaments caused the active force of the sarcomere. However, since then another protein called titin has been found to play important roles in modulating active force production as in stabilizing the sarcomere structure. The purpose of this experiment is to determine the effect of removing titin on the sarcomere structure and function. Specifically, we will test the hypothesis that the reduction in lattice spacing when muscle is stretched from a short sarcomere length to a long sarcomere length is due to the radial component of titin-based passive tension. To conduct this experiment, we must prepare the bundles of 3-10 fibers. Once prepared, we have to mount them between a force transducer and a motor in a physiological bath that allows simultaneous measurements of x-ray diffraction patterns and force while controlling muscle length. The mice have been genetically engineered to have a TEV protease binding site on titin that allows the TEV protease to bind and the titin to be cleaved in an adult muscle. We will measure d10 interfilament lattice spacing and equatorial intensity ratio, |11/|10., from the equatorial part of the X-ray diffraction patterns. Changes in these patterns will be used to assess changes in sarcomere structure when titin is cleaved by TEV protease.

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