Binding affinity is typically reported as equilibrium dissociation constant (KD). The smaller the KDvalue, the greater the binding affinity of the ligand for its target.
P + L <===> PL
KD = [P] [L] / [PL]
( P : protein ; L : ligand )
From cuves it is clear clear that : KD(TRG) > KD (DOT)
Thus affinity for DOT is greater than TRG.
fraction saturation , θ = [PL] / [P]+ [PL]
OR θ = [L] / [L]+KD
1.00 0.75- fractional saturation 0.50 0.25- 0.00 0 T 7 1 2 3 4 5 6...
1 2 3 4 5 6 7 8 9 Part A Which of the following is/are means whereby a catalyst can lower the activation energy of a reaction? quantum tunneling decreasing the number of reactive molecules permanently binding substrates inefficient collisions altering the temperature within the cell to one appropriate for reactions to proceed Subrnit Request Answer Part A An enzyme Obinds substrates in a manner that facilitates the formation of product decreases the rate of a reaction. is always...