@@dorothyotogbolu6485 lmao im an internet stranger who is studying biochem rn-and was wondering if you had become a doctor after seeing ur comment since u said ur studying MCAT which would mean if u did aight and didnt flop ur gpa prop in med school/gl to ya if ur not tho
That moment when you roam all websites and youtube channels to understand a specified information and literally none talk about it... then you find AK LECTURES simplifying your every doubt and question... seriously.. I'm really amazed. Thank you so much!
Andrey, you deserve a Nobel Peace Prize for your contribution to the knowledge of mankind ! You are very gifted a teacher ! When I graduate from med school, you might not be awarded yet but you will receive my donation!
you are a great man .. your explain is amazingly better than my professor 👏🏻👏🏻👏🏻👏🏻👏🏻👏🏻👏🏻👏🏻👏🏻👏🏻👏🏻👏🏻👏🏻👏🏻👏🏻👏🏻👏🏻👏🏻👏🏻👏🏻👏🏻👏🏻👏🏻thank you very much .. you save my life🤣🤣🤣🤣🤣🤣🤣
Hello, would you please help to understand the steady stand conditions where S0 is higher then this mentionned on the curve of Michaelis (initial substrate concentration is small)
What is the problem with using regular rate law to explain the catalysis reaction? Can't we use experiments to determine the order of the reaction? Is it because enzymes are not considered reactants but their concentration actually changes the rate of reaction?
when you explained on the Km constant, you said its units are concentration but isnt that mathematically incorrect because the units cancel out?? at 15 mins.
I have a question regarding steady state, how can enzyme-substrate complex remain constant if it increases throughout the graph? Thank you for your videos.
only the rate of reaction and the concentration of substrate increases throughout the graph. For the enzyme-substrate complex, its like work shifts in this certain analogy. You send someone to work at a place for an hour, then, when one hour has passed, that person leaves the place and you send someone else to go work at that place since that place is free, someone can take the spot to work. Two people can't work at that same place, but at the same time, if the place is empty then fill the job if you can. That way the number of people who work at that place stay constant (the concentration of people at that place stays constant), since only one person can be there at any time. If one person leaves, one enters, and the cycle goes forever...
rate of enzyme = rate of rxn ... only if the reaction cannot occur without the enzyme. (otherwise there will be a basal reaction rate, and enzyme increases the rate of the reaction, and hence "enzyme rate" is a difference of those two). So, we're basically assuming that reaction doesn't occur without the catalysts. Am I understanding that right?
+MimicIsaac i think the answer to that question is, E+S is a new reaction entirely, and you can calculate enzyme rate by just studying that reaction ... without considering what happens when S -> products by itself.
The mathematics makes complete sense but I'm a little confused with how you can assume a steady-state condition. To elaborate: this equation is derived assuming a very specific condition where K1 = K-1+K2. Of course, this is not the case everywhere. For example, if [S] >> [ES] >>>> [E]+[P], then, in my mind, it seems as though it's impossible for K1 = K-1+K2. In these initial conditions, for K1 to equal K-1+K2, you'd have to assume that the catalytic activity of the enzyme corresponds to the binding affinity of the substrate. This is not the case (is it?). Then using an equation we derived in these steady-state conditions, we somehow extrapolate the chemical behavior of these enzymes under other conditions! Like, how can we just assume that we can model enzymatic behavior at Vmax when the conditions are completely different in a situation where we can even begin to talk about Vmax? Any response is appreciated. I feel like I'm missing something fundamental here.
He's basically teaching the MCAT topics for free. this dude is amazing!
So Dorothy are u a doctor now I hope so lol
Anime and Stuff who are you? Soon though. I will definitely let you know.
@@dorothyotogbolu6485 lmao im an internet stranger who is studying biochem rn-and was wondering if you had become a doctor after seeing ur comment since u said ur studying MCAT which would mean if u did aight and didnt flop ur gpa prop in med school/gl to ya if ur not tho
That moment when you roam all websites and youtube channels to understand a specified information and literally none talk about it... then you find AK LECTURES simplifying your every doubt and question... seriously.. I'm really amazed. Thank you so much!
I hope you have a desk in some university, because i think you totally deserve one. More than my teacher for sure ahah
Andrey, you deserve a Nobel Peace Prize for your contribution to the knowledge of mankind ! You are very gifted a teacher ! When I graduate from med school, you might not be awarded yet but you will receive my donation!
"and so what that meeeeans is.. " lmao i love this man
maya maya hahahahahaha
Can we take a moment to appreciate how this flawless explanation is made in one single take? 👏👏👏
You are totally good at what you're doing. You're making life with biochemistry bearable for some of us. Thank you so much!!!
Give this man an award!
Seriously he deserves it !!
Best videos out there. I’ve been watching theses since I took anatomy in high school!! Amazing
you are amazing in explaining and simplifying complex concepts
Thank you so much
Your explanation is so simple and logical. Thank you very much!
You got me through organic chemistry. Thank you so much!
wow! your lectures are really helpful. what my teacher couldn't make me understand you make it crystal clear.
Thank you for going above and beyond to make these concepts easier. But it would've been even more amazing if you had a link for your lecture notes.
Wow, So amazing, thank u AK lectures hope you deserve my rewards 🎉🎉🎉
thanks so much professor AK Lectures you are such a blessing in my life.
I love your teaching style sir. Your channel really help me a lot. Thank you sir!!!
You are the GOAT! Clear, Concise, and well explained
CCWE!!
Aah were have you been my whole life! great lecture. Thank you!
God bless your soul this is the best explanation I've seen so far.
God bless you andrey ... it is very clear and logic
Awesome lecture! Thank you:)
Why do I even go to my lectures! :D
same question to myself :)
Beautifully explained. Thank you
superb way of expalining .... it helped me a lot.................thanx for making such amazing lecture videos
You make biochemistry look so easy.. Kudos 👍
Best youtube channel ever.... thank you so much for the video !!!
you are a great man .. your explain is amazingly better than my professor 👏🏻👏🏻👏🏻👏🏻👏🏻👏🏻👏🏻👏🏻👏🏻👏🏻👏🏻👏🏻👏🏻👏🏻👏🏻👏🏻👏🏻👏🏻👏🏻👏🏻👏🏻👏🏻👏🏻thank you very much .. you save my life🤣🤣🤣🤣🤣🤣🤣
Thanks for such a great lecture
amazing video. thank you so much
great explanations
I really hope everyone seeing these videos is ackowledging the value of fee education. The quality is top
You really has a very clear intonation and it helps me to understand as a non english speaker 😅
Great lecture,well presented
Your videos are awesome. 💞
u r amazing! Thank you so much
You are just excellent!
you are the best person i know
Congratulations from your pronunciation, easy to understand for an italian like me :)
you are fantastic!
Amazing thank you
"So can we derive such an equation, and the answer is yes." Fuckin' genius guy over here
You are awesome.
Hello, would you please help to understand the steady stand conditions where S0 is higher then this mentionned on the curve of Michaelis (initial substrate concentration is small)
Excellent
thank you.
What is the problem with using regular rate law to explain the catalysis reaction? Can't we use experiments to determine the order of the reaction? Is it because enzymes are not considered reactants but their concentration actually changes the rate of reaction?
This CZcams channel is the best have ever seen in my life 🥲
I love your lectures, they are quite comprehensible. could you kindly make your board much clearer. i can barely see what you explain
Thank you sir
when you explained on the Km constant, you said its units are concentration but isnt that mathematically incorrect because the units cancel out?? at 15 mins.
I have a question regarding steady state, how can enzyme-substrate complex remain constant if it increases throughout the graph? Thank you for your videos.
only the rate of reaction and the concentration of substrate increases throughout the graph. For the enzyme-substrate complex, its like work shifts in this certain analogy. You send someone to work at a place for an hour, then, when one hour has passed, that person leaves the place and you send someone else to go work at that place since that place is free, someone can take the spot to work. Two people can't work at that same place, but at the same time, if the place is empty then fill the job if you can. That way the number of people who work at that place stay constant (the concentration of people at that place stays constant), since only one person can be there at any time. If one person leaves, one enters, and the cycle goes forever...
What’s equal at the equilibrium?
rate of enzyme = rate of rxn ... only if the reaction cannot occur without the enzyme. (otherwise there will be a basal reaction rate, and enzyme increases the rate of the reaction, and hence "enzyme rate" is a difference of those two). So, we're basically assuming that reaction doesn't occur without the catalysts.
Am I understanding that right?
+MimicIsaac i think the answer to that question is, E+S is a new reaction entirely, and you can calculate enzyme rate by just studying that reaction ... without considering what happens when S -> products by itself.
what is the unit of Km constant ?
The mathematics makes complete sense but I'm a little confused with how you can assume a steady-state condition. To elaborate: this equation is derived assuming a very specific condition where K1 = K-1+K2. Of course, this is not the case everywhere. For example, if [S] >> [ES] >>>> [E]+[P], then, in my mind, it seems as though it's impossible for K1 = K-1+K2. In these initial conditions, for K1 to equal K-1+K2, you'd have to assume that the catalytic activity of the enzyme corresponds to the binding affinity of the substrate. This is not the case (is it?). Then using an equation we derived in these steady-state conditions, we somehow extrapolate the chemical behavior of these enzymes under other conditions! Like, how can we just assume that we can model enzymatic behavior at Vmax when the conditions are completely different in a situation where we can even begin to talk about Vmax? Any response is appreciated. I feel like I'm missing something fundamental here.
same...
so I
Greaaattttt
Guys did he made a video about co factors ?
really useful! #ChBE440Lectur8:MoreReactionMechanisms:EnzymKinetics
Why didn't i find you before. My exam is tomorrow and i know nothing of this😫
My worried is about the final Micheals equation .i.e equ8 and equ9
five years ago someone knew this
you sooo goood
Boinnnnnnng!!!!!!!!!!!!!!!!!!!!!!!!
Terjemahinin ke bahasa Indonesia dong
all i can hear is: equation equal to equation number equation equation substrate equation number equation.... omg i am failing so hard :' (
+APOLOnl LOOOOOOOOOOOOOOOOL
+Niecey Weesey hahaha luckily i still passed my test xD i love AK lectures. i was studying as a beast that day and got a little tired at that point xD
+APOLOnl Congratulations!
come for me if you will. but this definitely was not the best explanation as most of these comments say.
the concept is clear but the writing is not clear to understand so the writing makes me boring so change and make writing clear.
The writing makes you boring? what
Wot