The Relationship of Force on Myosin Subfragment 2 Region to the Coiled-Coiled Region of the Myosin Dimer

Description:

The stability of myosin subfragment 2 was analyzed using gravitational force spectroscopy. The region was found to destabilize under physiological force loads, indicating the possibility that subfragment 2 may uncoil to facilitate actin binding during muscle contraction. As a control, synthetic cofilaments were produced to discover if the observations in the single molecule assay were due to the lack of the stability provided by the thick filament. Statistically, there was no difference between the single molecule assay data and the synthetic cofilament assay data. Thus, the instability of the region is due to intrinsic properties within subfragment 2.

Creator(s): Hall, Nakiuda M.
Creation Date: December 2011
Partner(s):
UNT Libraries
Collection(s):
UNT Theses and Dissertations
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Publisher Info:
Publisher Name: University of North Texas
Publisher Info: www.unt.edu
Place of Publication: Denton, Texas
Date(s):
  • Creation: December 2011
Description:

The stability of myosin subfragment 2 was analyzed using gravitational force spectroscopy. The region was found to destabilize under physiological force loads, indicating the possibility that subfragment 2 may uncoil to facilitate actin binding during muscle contraction. As a control, synthetic cofilaments were produced to discover if the observations in the single molecule assay were due to the lack of the stability provided by the thick filament. Statistically, there was no difference between the single molecule assay data and the synthetic cofilament assay data. Thus, the instability of the region is due to intrinsic properties within subfragment 2.

Degree:
Discipline: Biochemistry
Level: Master's
PublicationType: Master's Thesis
Language(s):
Subject(s):
Keyword(s): Myosin | force spectroscopy | Hypertrophic cardiomyopathy
Contributor(s):
Partner:
UNT Libraries
Collection:
UNT Theses and Dissertations
Identifier:
  • ARK: ark:/67531/metadc103322
Resource Type: Thesis or Dissertation
Format: Text
Rights:
Access: Public
Holder: Hall, Nakiuda M.
License: Copyright
Statement: Copyright is held by the author, unless otherwise noted. All rights Reserved.