Simulate setup U_RL_Ai_Bs
Here we will compare outcomes of the four alternative models for conditions when binding is moderately tight and the off-rate is intermediate. The isomerization is chosen to be slow here. I choose binding affinity of 107 M-1 and off-rate and isomerization constants of 50 s-1. R and RL are separated by 100 s-1 and R* or R*L - by 100 s-1 from corresponding species. Isomerization equilibrium is shifted 5:1 toward *-forms. The reverse isomerization rate is 1 s-1 to make kex =6 s-1 .
Location: Ai_Bs/
|
|
|
|
Simulate setup U_RL_Ai_Bs |
|||
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
| Direct and reverse titrations will look the same | Direct and reverse titrations will look very differently, indicative of the exchange in the the free R or L. | Direct and reverse titrations will look the same, indicative of the exchange in the complex | |
Back to Analysis of Direct and Reverse Titrations