you are so much better at explaining these concepts than my tenured professor at a nationally recognized research institution. Props and thanks for helping me pass biochem.
Would this not give the initial concentration instead of Kd. We would then use this initial concentration to solve for Kd using the equilibrium equation.
Not using 100% theta has a simple practical reason. As the curve inevitable slowly, asymptotically approaches 100% the 100% is hard to determine experimentally. The 50% value, however, is much more simple to determine.
I'm very surprised that this video doesn't have more views! By far the best explanation of these graphs I have seen thus far. Thank you!!!
you are so much better at explaining these concepts than my tenured professor at a nationally recognized research institution. Props and thanks for helping me pass biochem.
omg you save lives! you have no idea...shortest and best explanation ever thank you
Thanks so much for the video, saved me in the last day for my presentation
Brilliant video, thanks!
This is just amazing! Thanks :)
very nice explanation
Would this not give the initial concentration instead of Kd. We would then use this initial concentration to solve for Kd using the equilibrium equation.
So are Km and Kd similar? Km also substrate concentration at 0.5 Vmax. How are the two different?
Thanks a lot for the video, you are great at it.This helped me very much with my school stuff. Keep up the good work.
+Catalyst University good
very good video help me a lot
So a higher Ka would also mean tighter binding/higher affinity? Thank you
no problem
Nice video...Thank you very much.
Thank you!
how to get y-axis value?
you're fantastic
thanks was useful
Why use 50%?
why cant it be at 100% theta, completely saturated ?
Not using 100% theta has a simple practical reason. As the curve inevitable slowly, asymptotically approaches 100% the 100% is hard to determine experimentally. The 50% value, however, is much more simple to determine.