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Massachusetts Institute of Technology

Effects of cross-link and myosin motor concentrations on active muscle gel contraction time and extent

Abstract

dc:description.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.

Degree

thesis:*
Department dc:contributor.department
Massachusetts Institute of Technology. Department of Mechanical Engineering.
Grantor dc:publisher
Massachusetts Institute of Technology
Year dc:date.issued
2017

Author and committee

dc:creator, dc:contributor.*
Author dc:creator
  • Babcock, Joseph M. (Joseph Michel)
Advisor dc:contributor.advisor
  • Anette Hosoi.

Subjects

dc:subject × 1

Rights

dc:rights
Statement dc:rights
  • 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.
Language dc:language.iso
eng

Identifiers

dc:identifier.*
Handle dc:identifier.uri
http://hdl.handle.net/1721.1/112565
OAI identifier oai:identifier
oai:dspace.mit.edu:1721.1/112565

Chain of custody

source
Harvested from
MIT
Base URL
dspace.mit.edu/oai/request
Last updated
2026-07-22
Source record
OAI-PMH GetRecord
citation

Babcock, Joseph M. (Joseph Michel). Effects of cross-link and myosin motor concentrations on active muscle gel contraction time and extent. Massachusetts Institute of Technology, 2017. http://hdl.handle.net/1721.1/112565