Now showing items 1-4 of 4
A Long Helix from the Central Region of Smooth Muscle Caldesmon
(East Carolina University, 1991-07-25)
The central region of smooth muscle caldesmon is predicted to form α-helices on the basis of its primary structure. We have isolated a fragment (CT54) that contains this region. The hydrodynamic properties and the electron ...
Characterization of a caldesmon fragment that competes with myosin-ATP binding to actin.
(East Carolina University, 1993-08)
The protein caldesmon inhibits actin-activated ATP hydrolysis of myosin and inhibits the binding of myosin*ATP to actin. Afragment isolated from a chymotryptic digest of caldesmon contains features of the intact molecule ...
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 ...