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Tropomyosin Dynamics in Cardiac Thin Filaments: A Multisite Förster Resonance Energy Transfer and Anisotropy Study
(East Carolina University, 2008-06)
Cryoelectron microscopy studies have identified distinct locations of tropomyosin (Tm) within the Ca21-free, Ca21-saturated, and myosin-S1-saturated states of the thin filament. On the other hand, steady-state Förster ...
The Actin Binding Protein, Fesselin, is a Member of the Synaptopodin Family
(East Carolina University, 2008-07)
Fesselin is a natively unfolded protein that is abundant in avian smooth muscle. Like many natively
unfolded proteins, fesselin has multiple binding partners including actin, myosin, calmodulin and
α-actinin. Fesselin ...
The RXR-alpha C-terminus T462 is a NMR sensor for coactivator peptide binding
(East Carolina University, 2008-02-22)
The C-terminal activation function-2 (AF-2) helix plays a crucial role in retinoid X receptor alpha (RXRα)-mediated gene expression. Here, we report a nuclear magnetic resonance (NMR) study of the RXRα ligand-binding domain ...
Negative Charges at Protein Kinase C Sites of Troponin I Stabilize the Inactive State of Actin
(East Carolina University, 2008-01-15)
Alterations in the troponin complex can lead to increases or decreases in contractile activity. Most mutations of
troponin that cause hypertrophic cardiomyopathy increase the activity of cardiac muscle fibers. In at least ...
Conservation of the regulated structure of folded myosin 2 in species separated by at least 600 million years of independent evolution
(East Carolina University, 2008-04-22)
The myosin 2 family of molecular motors includes isoforms regulated
in different ways. Vertebrate smooth-muscle myosin is activated by phosphorylation of the regulatory light chain, whereas scallop striated adductor-muscle ...