Browsing Brody School of Medicine by Subject "Actin"
Now showing items 1-6 of 6
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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 ... -
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 ... -
Fesselin, an intrinsically disordered smooth muscle protein, organizes and stabilizes actin-myosin and myosin
(East Carolina University, 2014)Fesselin is an intrinsically disordered protein that is known to bind a large variety of cytoskeletal proteins. The proteins fesselin is known to bind include: actin (Leinweber et al. 1999), [alpha]-actinin (Pham et al. ... -
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 ... -
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 ... -
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) ...