Keyword Analysis & Research: steady state kd

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What is the difference between steady-state and kinetic determinations?

Data analysis: Steady-state affinity determination •Kinetic determinations give an independent value •Steady-state response levels give one value for affinity constants •Steady-state can be used for fast interactions where kinetics are not available f on ak k K on f dk k K Kinetics and affinity Affinity only [BiaCore]

How many times Kd (1) is required to reach steady state?

Approximate calculated times required to reach 99.9% of the steady state at analyte concentrations ranging from 0.01 to 100 times KD (1) . BIACORE AB BIACORE Technology Handbook. (1998).

What is steady-state affinity determination?

Data analysis: Steady-state affinity determination •Kinetic determinations give an independent value •Steady-state response levels give one value for affinity constants •Steady-state can be used for fast interactions where kinetics are not available f on ak k K on f dk k K

What is the dissociation constant (Kd)?

The dissociation constant (Kd) quantifies the equilibrium between a ligand (L) being free in solution and bound to a site in a protein (EL): It corresponds to the affinity which the ligand has for the binding site.


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