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Binding data from membrane preparations indicated the presence of two classes of binding sites with KD of 1.5 +/- 0.4 nM and 25.5 +/- 11.0 nM.
Biosensor libraries harness large classes of binding domains for construction of allosteric transcriptional regulators.
The Scatchard plot analysis demonstrates that two classes of binding sites are formed with the equilibrium dissociation constants.
Therefore, the use of several classes of binding molecules will make suitable crystal formation and the determination of their 3D structure more likely.
Scatchard analysis showed that two classes of binding sites existed in the SIN-imprinted polymers, with their dissociation constants estimated to be 7.257×10−5 and 3.828×10−3 mol l−1, respectively.
A concave upward plot is indicative of nonspecific binding, negative cooperativity, or multiple classes of binding sites.
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This class of binding proteins, both natural and synthetic, has a strong tendency to bind a preformed cleft using a convex binding interface (paratope).
Scatchard analysis predicted for a single class of binding sites with Kd=1.4 nM.
Designed Ankyrin Repeat Proteins (DARPins) represent a novel class of binding molecules.
Antibodies have long been regarded as the only class of binding proteins.
Although many biologically significant interactions involve association of identical subunits, a much larger class of binding events involves interactions of dissimilar partners.
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