Data on whole length myosin binding protein C stabilizes myosin S2 as measured by gravitational force spectroscopy
Data presented in this article relates to the research article entitled “Whole length myosin binding protein C stabilizes myosin subfragment-2 (S2) flexibility as measured by gravitational force spectroscopy.” (Singh et al., 2018) [1]. The data exhibits the purified skeletal myosin binding protein C...
Main Authors: | Rohit R. Singh, James W. Dunn, Motamed M. Qadan, Nakiuda Hall, Kathy K. Wang, Douglas D. Root |
---|---|
Format: | Article |
Language: | English |
Published: |
Elsevier
2018-06-01
|
Series: | Data in Brief |
Online Access: | http://www.sciencedirect.com/science/article/pii/S2352340918303536 |
Similar Items
-
The Relationship of Force on Myosin Subfragment 2 Region to the Coiled-Coiled Region of the Myosin Dimer
by: Hall, Nakiuda M.
Published: (2011) -
Stretching the Flexible Myosin II Subfragment Using the Novel Gravitational Force Spectroscope, and the Uncoiling of S2
by: Dunn, James W.
Published: (2010) -
Secondary Structure of the Novel Myosin Binding Domain WYR and Implications within Myosin Structure
by: Lynda M. Menard, et al.
Published: (2021-06-01) -
An investigation of myosin binding protein C mutations in South Africa and a search for ligands binding to myosin binding protein C
by: De Lange, W. J. (Willem Jacobus)
Published: (2011) -
Cardiac myosin binding protein-C phosphorylation modulates myofilament length-dependent activation
by: Ranganath eMamidi, et al.
Published: (2016-02-01)