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Zero-length crosslinking procedure with the use of active esters.
The advantage of this method versus one-step zero-length crosslinking is that only one component of the complex is exposed to the crosslinker, which eliminates complications arising from the formation of crosslinks among several proteins of a multicomponent complex. Expand
Muscle Contraction
The calcium and magnesium binding sites on troponin and their role in the regulation of myofibrillar adenosine triphosphatase.
The results suggest that Tn and TnC contain six divalent cation binding sites: two high affinity Ca-2+ binding sites that also bind Mg- 2+ competitively (Ca-2-Mg-2 + sites); two sites with lower affinity for Ca-1+ that do not bind M g-2+. Expand
Myosin alkali light chain and heavy chain variations correlate with altered shortening velocity of isolated skeletal muscle fibers.
Among fibers that contained a variety of myosin isozymes, differences in shortening velocities were correlated with the alkali light chain ratio, myOSin heavy chain type, or a combination of both. Expand
Reconstitution of troponin activity from three protein components.
Recovery of activity could only be achieved when the required components were mixed prior to removal of urea, suggesting that one or more of these proteins may refold improperly on removal of Urea unless the other components are present. Expand
Thin filament proteins and thin filament-linked regulation of vertebrate muscle contraction.
The relation of protein structure to function will be emphasized and the relation of various physiologically and histochemically defined fiber types to the proteins found in them will be discussed. Expand
Molecular mechanism of troponin-C function
ConclusionsThere is now a large body of evidence in support of the view that Ca2+ binding to the low affinity sites of TnC induces a movement of helices B and C away from helices A and D, thusExpand
Purification and properties of the components from troponin.
Proper procedures have been developed for purification of three of the four protein components usually found in skeletal muscle troponin preparations, and an apparent functional property of each has been defined. Expand
Cooperative binding to the Ca2+-specific sites of troponin C in regulated actin and actomyosin.
The finding that fluorescence titrations of Ca2+ binding to TnCDANZ bound to actin-tropomyosin exhibit a Hill coefficient of 1.4 in its presence indicates the existence of true positive cooperativity in metal binding to sites I and II. Expand