Structural dynamics of calmodulin-ryanodine receptor interactions: electron paramagnetic resonance using stereospecific spin labels
Abstract We have used electron paramagnetic resonance, with rigid and stereospecific spin labels, to resolve structural states in calmodulin (CaM), as affected by binding of Ca and a CaM-binding peptide (RyRp) derived from the ryanodine receptor (RyR), the Ca channel that triggers muscle contraction...
Main Authors: | Cheng Her, Andrew R. Thompson, Christine B. Karim, David D. Thomas |
---|---|
Format: | Article |
Language: | English |
Published: |
Nature Publishing Group
2018-07-01
|
Series: | Scientific Reports |
Online Access: | https://doi.org/10.1038/s41598-018-29064-8 |
Similar Items
-
Regulation of the cardiac ryanodine receptor by calmodulin
by: Sigalas, Charalambos
Published: (2009) -
Electron paramagnetic resonance studies of spin-labelled ethidium bromide DNA interactions
by: Keeble, D. J.
Published: (1986) -
An Estimation Technique for Spin Echo Electron Paramagnetic Resonance
by: Golub, Frank
Published: (2013) -
Exploring Intrinsically Disordered Proteins using Site-Directed Spin Labelling Electron Paramagnetic Resonance spectroscopy
by: Nolwenn eLe Breton, et al.
Published: (2015-05-01) -
Electron paramagnetic resonance study of molecular spin multiplets with s>1
by: Hebden, James Arthur
Published: (2011)