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The binding constant was found to be 0.77 × 104 M− 2.
The binding constant was found to be stable around 10 M−1 for all temperatures employed.
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Moreover, the values of binding constant were found to be in the range of 103 M− 1, which is indicative of groove binding between ticlopidine and calf thymus DNA.
Both Stern-Volmer constants and binding constants were found to increase with increasing dendrimer generation (Table 1).
The highest binding constants were found for XOS, which approximately matched the length of the TrCel7A active site (Table 1).
The dissociation constant was found to be 1.35 × 10−10 M using Langmuir binding model.
Lysine residues that showed greater than a 2-fold increase in their modification rate constants were found to be located in (i) the CaM binding domain (Lys399A and Lys405A), (ii) the linker region between CaM binding and AI domains (Lys441A), (iii) the AI domain (Lys474A) of CNA, and (iv) the Ca2+ binding regions (Lys73B), and (v) the CNA binding region (Lys91B) of CNB.
Moreover, the stoichiometry of the C4D-NADH complex formed was found to be 1 1 and the binding constant was calculated to be 3.74 × 105 M−105
The binding constant was calculated to be 4.57 × 104 M−104
The binding constant was determined as described previously [ 29].
Therefore, the temperature dependence of the binding constant was studied.
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