Nucleic Acid Binding and Unfolding Properties of Ribosomal Protein S1 and the Derivatives S1-F1 and m1-S1
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چکیده
منابع مشابه
Binding of S1(A1) and S1(A2) to F-actin.
The binding curve of myosin subfragment-1 (S1) to F-actin is not a simple hyperbola: at high concentrations of S1 the binding curve can be transformed into a linear plot ("normal" binding), but at small concentrations of S1 the binding complications deform the binding curve and produce nonlinear transforms ("anomalous" binding) [Andreev, O. A., & Borejdo, J. (1992) J. Muscle Res. Cell Motil. 13...
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where on the left hand side the coefficient of XrY s is βrβs. If n is a natural number then β(X) = β([n]X), where [n]X = [n]F X is the n-series. We alse have β(X)−1 = β([−1]X), where F ([−1]X,X) = 0 = F (X, [−1]X). In fact, for any non-zero q ∈ Z(p), we can make sense of [q]X and β(X) = β([q]X). Now recall the Araki and Hazewinkel generators vn, wn ∈ BP2pn−2 for which v0 = w0 = p and vn ≡ wn mo...
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We have determined the equilibrium constants for the binding of AEDANS-labelled S1 to S1-depleted 30S and 70S ribosomes. For "tight" ribosomes, the association of S1 increases with the sixth power of Mg2+ concentration, but for 30S subunits and "loose" ribosomes, there is virtually no dependence of the association on Mg2+ over the same concentration range, 2-10 mM in Mg2+. The binding of S1 to ...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1979
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1979.tb06293.x