Now showing items 1-5 of 5
The Interaction of Caldesmon with the COOH Terminus of Actin
(East Carolina University, 1991-10-25)
Caldesmon interacts with the NH2-terminal region of actin. It is now shown in airfuge centrifugation experiments that modification of the penultimate cysteine residue of actin significantly weakens its binding to caldesmon ...
The delta-14 Mutation of Human Cardiac Troponin T Enhances ATPase Activity and Alters the Cooperative Binding of S1-ADP to Regulated Actin
(East Carolina University, 2004-12-07)
The complex of tropomyosin and troponin binds to actin and inhibits activation of myosin ATPase activity and force production of striated muscles at low free Ca2+ concentrations. Ca2+ stimulates ATP activity, and at ...
Localization and Characterization of a 7.3-kDa Region of Caldesmon Which Reversibly Inhibits Actomyosin ATPase Activity
(East Carolina University, 1992-08-15)
Cleavage of caldesmon with chymotrypsin yields a series of fragments which bind both calmodulin and actin and inhibit the binding of myosin subfragments to actin and the subsequent stimulation of ATPase activity. Several ...
Calponin interaction with alpha-actinin-actin: evidence for a structural role for calponin.
(East Carolina University, 1999-12)
The purpose of this study was to address the paradox of calponin localization with a-actinin and filamin, two proteins with tandem calponin homology (CH) domains, by determining the effect of these proteins on the binding ...
Troponin-tropomyosin: an allosteric switch or a steric blocker?
(East Carolina University, 2002-08)
The interaction of myosin subfragment 1 (S1) with actin-tropomyosin-troponin (regulated actin) is highly nucleotide dependent. The binding of S1 or S1-ADP (but not S1-ATP nor N,N - -phenylenedimaleimide-modified S1-ATP) ...