Fluorescence labeling and computational analysis of the strut of myosin's 50 kDa cleft.
In order to understand the structural changes in myosin S1, fluorescence polarization and computational dynamics simulations were used. Dynamics simulations on the S1 motor domain indicated that significant flexibility was present throughout the molecular model. The constrained opening versus closin...
Main Author: | Gawalapu, Ravi Kumar |
---|---|
Other Authors: | Root, Douglas D. |
Format: | Others |
Language: | English |
Published: |
University of North Texas
2007
|
Subjects: | |
Online Access: | https://digital.library.unt.edu/ark:/67531/metadc3974/ |
Similar Items
-
Columellar strut graft in unilateral cleft nasal deformity: Anthropometry and clinical outcomes
by: Kumar Prasad Preetha Rani, et al.
Published: (2019-01-01) -
Multifaceted Function of Myosin-18, an Unconventional Class of the Myosin Superfamily
by: Zhaohui Ouyang, et al.
Published: (2021-02-01) -
Fluorescence spectra of cardiac myosin and in vivo experiment: studies on daunorubicin-induced cardiotoxicity
by: Yang Liu, et al.
Published: (2015-12-01) -
Study on Strut and Node Behavior in Strut-and-Tie Modeling
by: Rezaei, Nazanin
Published: (2018) -
The 133-kDa N-terminal domain enables myosin 15 to maintain mechanotransducing stereocilia and is essential for hearing
by: Qing Fang, et al.
Published: (2015-08-01)