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The fused ring compound, DB2297, binds very weakly to ATGA, and the binding constants are not in the instrument's range for binding analysis.
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The increased magnitude of the binding constant was not significantly changed when the number and position of the modification in TFO changed.
However the correlation of extraction efficiency with binding constant was not linear.
The binding constants were calculated using Origin provided by ITC200.
EGF binding constants were based on experimental measurements.
The binding constant was determined as described previously [ 29].
Therefore, the temperature dependence of the binding constant was studied.
The Michaelis-Menten binding constant (KM) was not significantly changed by the C-terminal modification of actin (Table 2), showing that the apparent affinity for active cross-bridges was not affected by the modification of actin.
While the kinetic constants for substrate binding are not unusual, both enzymes had surprisingly low turnover rates.
Although the affinity constants for the tighter binding peptides are not well defined due to the high concentration of protein required for the NMR experiment, they are, nonetheless, broadly consistent with the additional contributions of the second and third phosphosites measured by ITC.
These are constant through many of the structures involving fucose binding and are not likely to change significantly in solution.
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