2026-09-19T12:58:46Zhttps://dspace.mit.edu/server/oai/requestoai:dspace.mit.edu:1721.1/1125652022-01-13T07:54:05Zcom_1721.1_7582com_1721.1_7581col_1721.1_131024
Anette Hosoi.
Babcock, Joseph M. (Joseph Michel)
Massachusetts Institute of Technology. Department of Mechanical Engineering.
Massachusetts Institute of Technology. Department of Mechanical Engineering
2017-12-05T19:18:33Z
2017-12-05T19:18:33Z
2017
2017
http://hdl.handle.net/1721.1/112565
1013187538
Thesis: S.B., Massachusetts Institute of Technology, Department of Mechanical Engineering, 2017.
Cataloged from PDF version of thesis.
Includes bibliographical references (page 26).
The cytoskeleton is a crucial network of actin filaments that gives the cell its shape, assists in organelle organization, and allows for cell movement. Active muscle gels are a class of materials that that mimic the functionality of the cytoskeleton. Utilizing myosin II motor proteins to initiate contraction events in actin networks, active muscle gels have the unique potential of acting as microscopic actuators. Two challenges currently faced by active muscle gels are their slow contraction time and weak contraction forces. This thesis seeks to achieve contraction events in a lab setting and observe how contraction speed and extent varies with the concentration of myosin motors and alpha-actinin crosslinks.
by Joseph M. Babcock.
S.B.
26 pages
eng
Massachusetts Institute of Technology
MIT theses are protected by copyright. They may be viewed, downloaded, or printed from this source but further reproduction or distribution in any format is prohibited without written permission.
http://dspace.mit.edu/handle/1721.1/7582
Mechanical Engineering.
Effects of cross-link and myosin motor concentrations on active muscle gel contraction time and extent
Thesis
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Publication
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<Abstract>The cytoskeleton is a crucial network of actin filaments that gives the cell its shape, assists in organelle organization, and allows for cell movement. Active muscle gels are a class of materials that that mimic the functionality of the cytoskeleton. Utilizing myosin II motor proteins to initiate contraction events in actin networks, active muscle gels have the unique potential of acting as microscopic actuators. Two challenges currently faced by active muscle gels are their slow contraction time and weak contraction forces. This thesis seeks to achieve contraction events in a lab setting and observe how contraction speed and extent varies with the concentration of myosin motors and alpha-actinin crosslinks.</Abstract>
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