Binding affinity is typically measured and reported by the equilibrium dissociation constant (KD), which is used to evaluate and rank order strengths of bimolecular interactions. The larger the KD value, the more weakly the target molecule and ligand are attracted to and bind to one another.
Kd is defined as dissociation constant that accounts for amount of reactant that dissociates reversibly to form component products; the constant deals with half of binding site of enzyme that binds for concentration of ligands, or the concentration for ligands that bind enzyme to be equal to that that are not; the unit
Kd = [A][B] [AB] For bimolecular reactions, the units of Kd are concentration (M, mM, µM, etc.)
How to calculate your KD ratio? KDA = (kills + assists)/ deaths, for your kill-deaths/assists ratio. That means, if a player has 10 kills and 5 deaths, his KD ratio is equal to 2. A KD ratio of 1 means that the player got killed exactly as many times as he successfully eliminated his opponents.
What would one expect to be a good KD value? Most antibodies have KD values in the low micromolar (10–6) to nanomolar (10–7 to 10–9) range. High affinity antibodies generally considered to be in the low nanomolar range (10–9) with very high affinity antibodies being in the picomolar (10–12) range.
The strength of a given interaction can be judged through the association constant K or the dissociation constant Kd. Very roughly, and taking 1 M as the reference standard state concentration: – Low affinity: Kd larger than 10–4 (> 100 microM) – Moderate affinity: Kd between 10–4 and 10–7 (100 microM – 100 nM)
The ratio Km / Kd is equal to the partition function of the assumed two-state-system. For the average enzyme, the partition function of the transition tends to equal 1 thus the majority of the substrate molecules are in the ground state and the assumption kcat << k-1 is valid hence Km ≈ Kd.
The EC50 is the drug concentration at which the drug is half-maximally effective. For the semi-log plot, the EC50 is the midpoint or inflection point of the curve. When the relationship between receptor occupancy and response is linear, KD = EC50.
KD is just the concentration of [L] that gives Y = 0.5 (half fractional saturation). –1/ KD. This is a useful transformation of the original hyperbolic binding curve to a simple line, from which the dissociation constant can be readily obtained.
The dissociation constant, KD, is the concentration at which 50% of the binding sites (receptors) are occupied by the drug. Occurs when an antagonist binds to the receptor in a site different from the binding site of the agonist.
KD. Kill Death Ratio (gaming)
KA = 1/ KD = 1010 M-1.
80-1.00 is average and anything about 1.00 is good. If you at least have a 1.00 KD it means you’re killing more than you’re dying.
Anything above 1.0 is good, but 2.0 or 3.0 is preferable. Even if you’re playing Montagne and don’t directly engage the enemy very much, the times when you do have to fight an enemy, you need to be able to keep that 1.0 K/D.
You need minimum 6750 kills without any death to have 2.0, so if you have 2.0 kd any game you will need about 3000 kills, 15 per game is 200 games.