The Binding Constant of ATP to Myosin S1 Fragment
نویسندگان
چکیده
منابع مشابه
Effects of ATP and actin-filament binding on the dynamics of the myosin II S1 domain.
Actin and myosin interact with one another to perform a variety of cellular functions. Central to understanding the processive motion of myosin on actin is the characterization of the individual states along the mechanochemical cycle. We present an all-atom molecular dynamics simulation of the myosin II S1 domain in the rigor state interacting with an actin filament. We also study actin-free my...
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The protein caldesmon inhibits actin-activated ATP hydrolysis of myosin and inhibits the binding of myosin.ATP to actin. A fragment isolated from a chymotryptic digest of caldesmon contains features of the intact molecule that make it useful as a selective inhibitor of the binding of myosin.ATP complexes to actin without having the complexity of binding to myosin. The COOH-terminal 20 kDa regio...
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Apotransferrin (apo Tf) in 0.1 M N-(2hydroxyethyl)piperazine-N2-ethanesulfanic acid at 25 ˚C and pH 7.4 has been titrated with acidic solution of Tb3+. The binding of Tb3+ at the two specific metal-binding sites of transferrin was followed from the changes in the difference UV spectra at 245 nm. The molar absorptivity per binding site for Tb3+...
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Equilibrium measurements of the rate of binding of caldesmon and myosin S1 to actin-tropomyosin from different laboratories have yielded different results and have led to different models of caldesmon function. An alternate approach to answering these questions is to study the kinetics of binding of both caldesmon and S1 to actin. We observed that caldesmon decreased the rate of binding of S1 t...
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The human hypertrophic cardiomyopathy mutation R453C results in one of the more severe forms of the myopathy. Arg-453 is found in a conserved surface loop of the upper 50-kDa domain of the myosin motor domain and lies between the nucleotide binding pocket and the actin binding site. It connects to the cardiomyopathy loop via a long α-helix, helix O, and to Switch-2 via the fifth strand of the c...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1977
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1977.tb11742.x