This guy is an absolute genius and explains everything perfectly. You can watch it over and over again until you get it and even in fast forward when you are just reviewing. This is the future of education.
Wow. 3 hours in lecture and I didn't understand this...and in just 14 mins of watching this video, I feel like an expert in this lol. AMAZING WORK! My teachers should be more like this guy
Wish I hadn’t found this so late in the semester but also glad I found it before finals. Thank you for being so articulate! I never thought I’d understand this.
I can see why there are so many confused people here. Rather than this being one reaction, it should be looked at as data from a set of reactions (experimentss) whereby the only thing differing in each experiment is the concentration of the substrate, starting with low concentration and increasing it with each reaction. That is how the curve is formed, and I really think that should have been explained at the start to avoid confusion.
Yes, thats the first mistake I saw in his videos. In 11:18 he says: " At the end of the reaction when we have a very very high concentration." implying that the diagram describes the time sequence of one reaction. But apart from that dude youre the best tutor I know
X-axis is the concentration of substrate....when we assayed the enzyme substrate solutions we recorded the change in absorbance over time. One assay to find the best concentration of enzyme, to use for the second assay. Then the second assay using a fixed amount of enzyme and varrying concentration of substrate/buffer. In the second assay we measured abs every 15 sec for 2 min straight, did this for each concentration prepared in mM(adding enzyme right before the assay). We plotted umol/min on the y-axis, eventually but this(MMeq. Graph) is the 3rd out of 4 graphs that we needed for the one experiment, to analyze our results. Pretty crazy stuff, right! No way he could do the whole explination of the expirement in one video lol, I thought it was a good video for MM eq.
Excellent presentations available world wide 24/7/365. Truly a teaching revolution, much appreciated!👍 Improvement suggestion: downloadable Excel file of the equation.
Literally studying for the MCAT biochemistry and you just taught me better than what my intro biochem prof couldn't. In less than 2 hours... more so less than 15 minutes. Thank you!
Lord Pumpernickel lass dich nicht unterkriegen von den lehrern, die haben die sicht auf die jugend verloren und können sich nicht in sie hineinversetzen (nur wenige) power durch die 11. und 12 und danach kannst du studieren, was viel leichter ist, wenn man auch mehr Stoff zu lernen hat!
I am turkish. I'm a chemistry student. I study chemistry at the best university in my country. But I do not understand them. Unfortunately my english is not enough. It is hard to find a Turkish course book. The work you do is very successful. Hope one day we will have trainers like you. I feel very sorry for my country. Thank you
They gave u 3 lessons for this typa university u go to. All of michaelis mentin kinetics was covered in 1 lesson for me including competitive noncompetitive and uncompetitive inhibition.
i was soo apprehensive about this concept but your soo proficient that you made this concept succinct easy for me to understand it better. thank you soo much sir. your efficient in your elucidation.
Thank you so much! I have a final exam in a few days were i need to explain and justify different mathematical/biological functions and equations. Now i can cross one out. Thanks!
when t = 0, wouldn't that mean that the system is saturated in substrate since the substrate did not bind to the enzyme to form a product? (E + S ES E + P) The graph is initial Velocity with respect to Substrate Concentration, so what does time have to do with anything in the examples? Shouldn't we just assume when Substrate Concentration is very low? Thank You
Thank u so much.your lectures are just perfect.it makes me understand my teacher notes as well.and I first watch your lectures then start reading my teacher notes and it's too much easy for me to understand them without any difficulty😊
Basically a fancy way of saying that when the reaction velocity of a certain enzymes is at the max, no matter how much more you throw substrate at it, it won't react to the additional substrate
In some textbooks, they tell you to simply take the inverse of the x-axis and inverse of the y-axis, because given that it's impossible to find the exact value of Vmax (being that's it's asymptotic), when you do a double-reciprocal, where the x-axis is 1/S and the y axis is 1/V, the value of 1/Vmax is the point touching the y-axis, and the value of -1/Km is the point touching the x-axis. You can calculate the values of Vmax and Km from that.
Here's what I don't understand, If while deriving the MM equation we have to make the assumption that we are only looking at t approximately equal 0, then why can we continue to use the equation to describe V naught when time does not equal zero?
Good video, but you are mixing up the x-axis of [s] with a time scale. The time scale is important to consider to make sure you maintain the steady state condition for the M-M kinetics (i.e. [s] has not appreciably been depleted over time)
So we said "at the begining [S]=0 (approximately) so we neglact it and get V0= Vmax/Km [S] " I get it but can't we just put [S]=0 in here and get V0= 0?
Looking at it in retrospect it is the same thing but wouldnt it be better if we could assume S=Km and not the other way round :-/ okay yes granted that we need to define Km and not S so we did what we did but that should be used to give a better explanation.
I have a question! Why does steady state assumption only apply to enzymes, not to inorganic catalyst? I understood this that inorganic catalyst has rate-determining step, but enzymes don't. Why do enzymes don't have a slow step? Is it because of the structure of enzymes? It would be really helpful if you could answer me!
I do not understand why we can make all of these assumptions. Why can we just assume that the Km value is equal to [S]? We derived the Km value from three K constants of three different reaction, therefore we can conclude that it is a constant as well. Why is this constant equals to [S]...? Additionally you said that since Km is in the denominator with [S] then it has to have the same units. How is that statement even true? Sorry, experiencing a lot of frustration with this subject, and that statement + Assumptions are just causing confusion.. Anyone knows how to actually intuitively understand this equation?
I am confused is V naught the same thing as just rate? (V) I am confused because some people just say "rate" when they are talking about V naught.. What is the difference between the two?
I am asking because V naught is represented in the Y. Does that mean that the higher the scale, the V naught's value increases (like many graphs) or is the V naught constant? Some graphs state that the V naught has a directly proportional relationship with [S] but if V naught is stated as constant, (aka same value) how could it increase? Sorry if this a confusing question
when t = 0, shouldn't it start from high substrate to low substrate concentration? or in other words, it should start from the right to the left of the graph, right?
It means addition of substrate, lesser substrate being added up in beginning that's why it says zero order at end coz substrate concentration is so high that all available active sites have been saturated
So here’s my new method: disregard everything my lecturer says and head straight here. It works. Love this guy.
This guy is an absolute genius and explains everything perfectly. You can watch it over and over again until you get it and even in fast forward when you are just reviewing. This is the future of education.
How does he draw lines so straight on a whiteboard... He's so powerful.
Wow. 3 hours in lecture and I didn't understand this...and in just 14 mins of watching this video, I feel like an expert in this lol. AMAZING WORK! My teachers should be more like this guy
Second year of med school and still watchin your videos! Thank you for makin my Life so much easier!!!
how does it feel to be a doctor now?
You do a hell of a job dude, thank you so much for these videos.
Man, you are absolutely gifted in teaching. We appreciate you. Thank you.
Wish I hadn’t found this so late in the semester but also glad I found it before finals. Thank you for being so articulate! I never thought I’d understand this.
I can see why there are so many confused people here. Rather than this being one reaction, it should be looked at as data from a set of reactions (experimentss) whereby the only thing differing in each experiment is the concentration of the substrate, starting with low concentration and increasing it with each reaction. That is how the curve is formed, and I really think that should have been explained at the start to avoid confusion.
I noticed that as well at the beginning and scrolled down the comments for verification. Thanks.
Yes, thats the first mistake I saw in his videos. In 11:18 he says: " At the end of the reaction when we have a very very high concentration." implying that the diagram describes the time sequence of one reaction. But apart from that dude youre the best tutor I know
My concentration level plump after 11 minutes with anything related to Michaels menten... not just ak hahah. But good point though
He explains that in the previous video that is the precursor to this video in his playlist for enzymes
X-axis is the concentration of substrate....when we assayed the enzyme substrate solutions we recorded the change in absorbance over time. One assay to find the best concentration of enzyme, to use for the second assay. Then the second assay using a fixed amount of enzyme and varrying concentration of substrate/buffer. In the second assay we measured abs every 15 sec for 2 min straight, did this for each concentration prepared in mM(adding enzyme right before the assay). We plotted umol/min on the y-axis, eventually but this(MMeq. Graph) is the 3rd out of 4 graphs that we needed for the one experiment, to analyze our results. Pretty crazy stuff, right!
No way he could do the whole explination of the expirement in one video lol, I thought it was a good video for MM eq.
Excellent presentations available world wide 24/7/365. Truly a teaching revolution, much appreciated!👍
Improvement suggestion: downloadable Excel file of the equation.
You are awesome!! Very organized, clear, and to the point.
literally learning biochem completely from your lectures, thank you so much for your work
Literally studying for the MCAT biochemistry and you just taught me better than what my intro biochem prof couldn't. In less than 2 hours... more so less than 15 minutes. Thank you!
im from germany and in the 11 grade right now and still understand from u in english more than my teacher in german gg :D
Lord Pumpernickel lass dich nicht unterkriegen von den lehrern, die haben die sicht auf die jugend verloren und können sich nicht in sie hineinversetzen (nur wenige) power durch die 11. und 12 und danach kannst du studieren, was viel leichter ist, wenn man auch mehr Stoff zu lernen hat!
One request plz never stop making such amazing videos
Plz
It really helps
Helps a lot
I am turkish. I'm a chemistry student. I study chemistry at the best university in my country. But I do not understand them. Unfortunately my english is not enough. It is hard to find a Turkish course book. The work you do is very successful. Hope one day we will have trainers like you. I feel very sorry for my country. Thank you
Great job! I'm not a native english speaker so your good pronunciation really helps. Thank you!
i clapped everytime after your videos :D
hah! thanks Andy! much appreciated!
Your videos are helping me study for the MCAT, THANK YOU! 🙏🏼
But these lectures are for mainly postgraduate students not for intermediate
3 lessons and i understood none, 14 minutes and i understood everything, mind blowing. Keep it up you are a genious, thank you.
They gave u 3 lessons for this typa university u go to. All of michaelis mentin kinetics was covered in 1 lesson for me including competitive noncompetitive and uncompetitive inhibition.
you just saved my biochem grade...
You're a legend. You should be nominated for a Nobel Peace prize.
i was soo apprehensive about this concept but your soo proficient that you made this concept succinct easy for me to understand it better. thank you soo much sir. your efficient in your elucidation.
Thank you so much! I have a final exam in a few days were i need to explain and justify different mathematical/biological functions and equations. Now i can cross one out. Thanks!
Gorgeous explanation!! I keep coming back for more of your videos! Thank you from the bottom of my heart!! You help me quite a bit.
YOU ARE AMAZING!! Biochem has never been easier
You deserve more than this number of subscribers
amazing video. Made so much sense after this. Getting me through my biochem class
Your explanation is wonderful.... Thank you
when t = 0, wouldn't that mean that the system is saturated in substrate since the substrate did not bind to the enzyme to form a product? (E + S ES E + P)
The graph is initial Velocity with respect to Substrate Concentration, so what does time have to do with anything in the examples? Shouldn't we just assume when Substrate Concentration is very low?
Thank You
You are the best instructor I have had in college lol. Thank you so much for your videos!
Thank you, SOOOOO much!! Only 14:14, made more sense than the 10hrs I spent already trying to figure out my biochem hw.
This guy continues to save my life.
Kudos Sir. U r God-Gifted❤️
Thank u so much.your lectures are just perfect.it makes me understand my teacher notes as well.and I first watch your lectures then start reading my teacher notes and it's too much easy for me to understand them without any difficulty😊
Basically a fancy way of saying that when the reaction velocity of a certain enzymes is at the max, no matter how much more you throw substrate at it, it won't react to the additional substrate
You are an excellent teacher. God bless you.
In some textbooks, they tell you to simply take the inverse of the x-axis and inverse of the y-axis, because given that it's impossible to find the exact value of Vmax (being that's it's asymptotic), when you do a double-reciprocal, where the x-axis is 1/S and the y axis is 1/V, the value of 1/Vmax is the point touching the y-axis, and the value of -1/Km is the point touching the x-axis. You can calculate the values of Vmax and Km from that.
Lineweaver burke plot.
A very great lecture Sir. Thank you very much. Namaste
I love your pedagogical skills ak. Keep on making such great videos. Love
thanks!
u just helped a desperate MSc student. Thank you
Definitely a life saver
i feel a sense of enlightenment after watching this lecture 😂
did anyone else hear the subtle police sirens at ~4:21? LOL
Flawless, just amazing. Thank you!
I swear he needs to be a professor. If he's not a professor.....I'll cry a river.
You are incredible. You make learning so much fun. Thank you so very much
no confusion....great combination sir... thnks a lot...
At 4:40 he says that "that gives us the y-coordinate, the Michaelis constant Km" but means the x-coordinate
Thank you respected Sr.
Your tutorials are top
Wasted my time seeing khan lecture of this equation!! Now watching AK and it makes so much sense.
Here's what I don't understand, If while deriving the MM equation we have to make the assumption that we are only looking at t approximately equal 0, then why can we continue to use the equation to describe V naught when time does not equal zero?
Why are you so awesome? I can't thank you enough.
i love this guy.
wow! what a wonderful explanation...
This is awesome :D I learned so much from your videos!
Very helpful videos thank you
Thank you for making this video. You really helped me.
A lot of respect for you sir 😍😍😍😍😍😍😚😚😚
Your videos are really helpful!
This video is so good tried to like it twice
Good video, but you are mixing up the x-axis of [s] with a time scale. The time scale is important to consider to make sure you maintain the steady state condition for the M-M kinetics (i.e. [s] has not appreciably been depleted over time)
getting me through biochemistry one video at a time
I love the way u teach...
this is exactly what i was looking for! thank you!
superb notes thanks
Thank u sir for helping me to understand this equation
at t0 the concentration of P is zero, not S. Km is not bigger than S at t0.
thank you so much!
Drinking game! Drink every time he says “at the beginning”
gonna binge your biochem videos until friday.. #finals
Massive respect !!!
Well presented!
Cheers, Andrey.
Thanks
So we said "at the begining [S]=0 (approximately) so we neglact it and get V0= Vmax/Km [S] " I get it but can't we just put [S]=0 in here and get V0= 0?
You are amazing!
why do you refer to the t=0 when referring to the condition [s]
Thank you so much you saved my marks :'-)
Looking at it in retrospect it is the same thing but wouldnt it be better if we could assume S=Km and not the other way round :-/ okay yes granted that we need to define Km and not S so we did what we did but that should be used to give a better explanation.
I have a question! Why does steady state assumption only apply to enzymes, not to inorganic catalyst?
I understood this that inorganic catalyst has rate-determining step, but enzymes don't.
Why do enzymes don't have a slow step? Is it because of the structure of enzymes?
It would be really helpful if you could answer me!
Excellent :)
Love and respect from Pakistan
great job!!!!
Thank you so much..
THANK YOU SO VERY MUCH
Thank you Sir
Can you explain what's the zero order reaction has to do with enzyme kinetic?our professor mentioned it but I didn't quite understand it
aweosome thank you
3:55, I realize this is a well-known equation, but how does (1x/2x) not equal simpy x/x? Instead of vmax over 2?
I do not understand why we can make all of these assumptions. Why can we just assume that the Km value is equal to [S]? We derived the Km value from three K constants of three different reaction, therefore we can conclude that it is a constant as well. Why is this constant equals to [S]...?
Additionally you said that since Km is in the denominator with [S] then it has to have the same units. How is that statement even true? Sorry, experiencing a lot of frustration with this subject, and that statement + Assumptions are just causing confusion.. Anyone knows how to actually intuitively understand this equation?
where’s the equilibrium and what’s equal at the equilibrium?
not all heroes wear capes after all
I am confused is V naught the same thing as just rate? (V) I am confused because some people just say "rate" when they are talking about V naught.. What is the difference between the two?
I am asking because V naught is represented in the Y. Does that mean that the higher the scale, the V naught's value increases (like many graphs) or is the V naught constant? Some graphs state that the V naught has a directly proportional relationship with [S] but if V naught is stated as constant, (aka same value) how could it increase? Sorry if this a confusing question
Why we do not get accurate reading of Vmax by Michaelis Menten graph ?
Can we write this in question realed to Uni substrate enzyme kinetics?
How is the Vmax value obtained?
By experiment?
when t = 0, shouldn't it start from high substrate to low substrate concentration? or in other words, it should start from the right to the left of the graph, right?
It means addition of substrate, lesser substrate being added up in beginning that's why it says zero order at end coz substrate concentration is so high that all available active sites have been saturated
Great job sir saluttteeee