It's incredible how you can actually teach more in a maximum of 22 minutes (part one and two of both vieos) way more detailed, accurate and precise CONTENT than a normal university lecture that lasts 50 minutes (I'm a biochemistry student). It seems that university teachers no longer know how to teach students
most university professors aren't there to teach. That's just something that is required, while the professors are there do actually do other things like research. So teaching isn't what they necessarily signed up for, but have to do so they can do their actual job (research).
Whenever my college mates ask me about the reason for I don't attend classes..my answer is:"I have AK lectures at home!"...but they don't understand what I mean unless they watch your videos...
its baffling how your 22 minute videos COVERED this is pure and uttermost detail, you talked about all the inhibition states and brought your point across. Honestly why didnt i find you in my first semester! you sir are the real GOAT
Thank you so much. Your amazing videos will be shared with as many as I can with my friends who are desperately looking for such videos. You are the MAN.
my hku space teacher is just a RUBBISH, GOMI desu. You must be a hard working student in the school day, digging into every details during your studies time, u will be highly respected and famous one day
Great videos! Thank you. Can I ask what the mechanism is which "kicks off" the competitive inhibitor when [S] is increased? The explanation that you give sounds like increasing [S] only affects chances of either [S] or [I] binding, not what happens when the inhibitor is already bound and [S] is increased thereafter.
Should have came here sooner! My university instructor does not explain this material this well then expects us to read and understand words without clear examples. I was so lost until I got here!
I have a question...towards the end of the lecture you mentioned about mixed inhibitions (4th type of inhibitors)..It's the same as noncompetitive inhibitors right?
Vmax stays the same in competitive inhibition because increasing the concentration of substrate will eventually lead to the Vmax as a higher increase of substrate outcompetes the competitive inhibitor. Since the substrate (at high concentration) outcompetes the inhibitor, the active sites of all the enzymes in the solution will virtually be sautrated with the substrate, not the inhibitor. Thus, Vmax can still be attained. Unlike competitive inhibition, uncompetitive inhibition causes a decrease in Vmax. Because the enzyme-substrate-inhibitor (ESI) complex cannot catalyze the reaction (synthesize products), and cannot be rescued by increasing substrate, the Vmax is lowered. So essentially the uncompetitive inhibitor is decreasing the overall number of active enzyme molecules in the solution.
It's incredible how you can actually teach more in a maximum of 22 minutes (part one and two of both vieos) way more detailed, accurate and precise CONTENT than a normal university lecture that lasts 50 minutes (I'm a biochemistry student).
It seems that university teachers no longer know how to teach students
most university professors aren't there to teach. That's just something that is required, while the professors are there do actually do other things like research. So teaching isn't what they necessarily signed up for, but have to do so they can do their actual job (research).
Amen to that!
Whenever my college mates ask me about the reason for I don't attend classes..my answer is:"I have AK lectures at home!"...but they don't understand what I mean unless they watch your videos...
its baffling how your 22 minute videos COVERED this is pure and uttermost detail, you talked about all the inhibition states and brought your point across. Honestly why didnt i find you in my first semester! you sir are the real GOAT
Wooow so glad my friend sent me this video. You explained this extremely well. Sent this to more people too.
You just helped out pharmacy students
Awesome! Best of luck with pharmacy school, I dont know how you guys do it with remembering all those meds! :)
You’re an angel
Thank you, a lecture from 9 years ago has a better way of explanation than current lecturers
Have shared your channel with my university peers :)
james fancourt Thats awesome, thanks a ton James :) Appreciate that.
I absolutely love your energy. The way you're passionate about the subjects you teach makes everything so much more enjoyable!
i am just shockeeeed!!!!!!!! THANK YOUUUU how can a single human know that much.. incredible
Thank you so much. Your amazing videos will be shared with as many as I can with my friends who are desperately looking for such videos. You are the MAN.
Very understable lectures and nearly I saw about 350 lectures in one months....👍👍👍👍
you are very best, you are the specific type of teacher that we poor students are looking for, some hku teachers are so worst
you are the best brother ever , God bless you !
by far the best explanation
Very good videos on inhibitors, ties in well with how they affect the enzyme paramaters in the line weaver burk plot video :)
james fancourt Thanks! I try to tie them all in, so it really helps to watch them in a consecutive order :)
Excellent video
Wonderful
Thanks a lot
your videos helped me so much to understand my enzyme course
Very much helpful.. Great lecture
my hku space teacher is just a RUBBISH, GOMI desu. You must be a hard working student in the school day, digging into every details during your studies time, u will be highly respected and famous one day
Thanks for this much detail, You are awesome! I wish u were my Biochemistry Lecturer
Great leactureeee
Really grt u helped me out in my exams tq....
You are the best professor on earth god bless you I truly envy your students 😩can you come and teach in my university?
Ok. Uncompetitive inhibition cannot be reversed increasing substrate concentration. Then, how can it be reversed? This inhibition is reversible, no?
thank u so much can u plz add the mixed inhibitors . ur vedio helps me alot in my study
that is literally awesome dude
you are so amazing!!
Why no product is formed in uncompetitive inhibition like non competitive inhibition?
Great videos! Thank you. Can I ask what the mechanism is which "kicks off" the competitive inhibitor when [S] is increased? The explanation that you give sounds like increasing [S] only affects chances of either [S] or [I] binding, not what happens when the inhibitor is already bound and [S] is increased thereafter.
Should have came here sooner! My university instructor does not explain this material this well then expects us to read and understand words without clear examples. I was so lost until I got here!
Great Videos. Thank you.
you can actually help and donate to him for his free lectures. His link is in description. It will motivate him.
I have a question...towards the end of the lecture you mentioned about mixed inhibitions (4th type of inhibitors)..It's the same as noncompetitive inhibitors right?
Competitive inhibition
Thank u😍
thankyou very much
thanx so much!!! totally understand...
nice lecture ...
thanh you , you are reallllllllly awosome 💗👨🏫
beautifully explained, thank you so much
who are we without you 😭🙏
Hi how can uncompetitive Inhibitors increase the affinity of the enzyme to substrate ?
Yes, as uncompetitive inhibitors lower the Km of the enzymes in the solution.
I love you bro
Well done but just mixed up uncompetitive and non competitive they should be replaced each other in this video
Hi, and wow!
but why does the Vmax stay the same in the competitive inhibition, and increases in the uncompetitive inhibition?
Vmax stays the same in competitive inhibition because increasing the concentration of substrate will eventually lead to the Vmax as a higher increase of substrate outcompetes the competitive inhibitor. Since the substrate (at high concentration) outcompetes the inhibitor, the active sites of all the enzymes in the solution will virtually be sautrated with the substrate, not the inhibitor. Thus, Vmax can still be attained. Unlike competitive inhibition, uncompetitive inhibition causes a decrease in Vmax. Because the enzyme-substrate-inhibitor (ESI) complex cannot catalyze the reaction (synthesize products), and cannot be rescued by increasing substrate, the Vmax is lowered. So essentially the uncompetitive inhibitor is decreasing the overall number of active enzyme molecules in the solution.