I'm taking a biochem class in college, I haven't learned a single thing from my lectures and you're saving me right now. I can't tell you thank you enough!
Thank you, Zack! Very comprehensively explained and yet easy to understand. This channel is one of the few that makes core concepts in biochemistry easy to follow. I’m reading Devlin’s biochemistry in sync with your videos. This channel for me is not just educational or informative which of course it is. It’s the ideal that you follow in taking such care to put top notch lectures out there that keeps me coming back nearly everyday at least in recent times. I’m planning on finishing all the lectures in a few months.
Sir ! you have an error ! you started the graph from Km ! the graph should start from 0 whatever was the type of inhibition, Km and Vmax are changing but the enzymatic reaction always start from 0. Thanks for your efforts and hardwork ❤
10k No Videos Challenge I think so there should be another line inthe graph which starts at the point 0 then goes and joins vmax line,but this line should be a little bit more curved ,so the Km will be higher and Vmax/2 will stay at the same point.(Cause vmax isnt changed)
Question! Since the Km is the concentration where half the Vmax is reached, why do the lines for all the inhibitions START at Km? I feel like they should all start at zero and it should be the slope of the curves that pushes the Km to the left or right!
it might be too late to respond to your question but you're right all slopes should start a 0 because when there is no substrate there is no rate of the enzyme. It needs a substrate to operate.
Sir i have no words to thank you, sir its very easy to understand you are amizing 😇sir iam from india from kerala state, mostly i cant never understant the foregin accent bt yr language is understandable nd easly to follow, thanks for being there to help us, 🙏😇
@@risconsiano, you’re incorrect. Km is the substrate concentration which will give us half of the maximum rate of reaction (velocity) for that specific enzyme. You can’t start at Km. You start at the origin, and then shift right going for your Vmax. Then you can find the new Km in that line. But you can’t use Km as the starting point. So the graph is incorrect, I think he just didn’t notice.
I'm speaking French I'm studying in Italy and I would work with you for helping me to buying my study. I'm able to translate ours video in Italian and French language. 😊 thank you so much
You video is very very helpfull ,thank you so much ,but i have just a small suggestion ,please after the lecture take a picture of all the board then put it here 🙏🏻🙏🏻 i want to study them😊 i hope the best for you❤
Dude, i have a huge confusion on that point, why are you starting the graph from the increased value of Km on x axis? shouldnt the graph still start from the zero (all three case)? because Km = [S] in half Vmax, help me please!
Thanks alot.You explained everything really well.Can you please explain y Km increases/stays the same (variation of Km) depending on nature of inhibitor?
quick question: on the graph drawn on the 9th minute 28 second shouldn't the graph start at the origin and cross the half Vmax dotted line at the same point and normal then not make it to Vmax ? so as to bring out the idea of no change in Km clarify on that
I don't understand😢, if the km increases which would lead to a corresponding decrease shouldn't the graph tend towards zero given that the km is negative and the decrease once in the negative becomes bigger?
If we need to extract invertase enzymes in the lab from saccharomyces yeast and give the sample for 3 students A,B and C , they extract in the same way Under the same conditions and the same chemical student (A) get 3*Km ،Student (B) get 2*Km , Student (C) get 1*Km , So, who extracts the highest amount of invertase ?
hey, i don't know if I understand it wrong. But at 10.14 he draws the line for N.C.I. the Km stays the same, but the km is not the start of the line right? It's when it's 0.5Vmax right? Now in the graf the Km of normal and non competitieve inhibition isn't the same.
Shouldn't all of lines in the Michaelis Menten graph all start at (0,0) and the trajectory will differ depending in the different types of inhibition. The way NN drew it it looks like they start before of after normal Km which is confusing.
I agree, he speaks very fast even for a native speaker. I have to pause the video a lot so I can comprehend what he says :). Keep in mind, he is speaking the language of biochemistry, which is a very dark language .. lolzz
What about Irreversibile Inhibitors? You talked about them in the last video but never mentioned if the change and how they change the Vmax or Km. Can someone help me understand it?
Because the substrate can’t bind to the enzyme, both Vmax. The substrate being unable to bind to the enzyme means no ES complex forms (affecting Vmax); the enzyme would have a much lower affinity to the enzyme (binding to the inhibitor) and I’m pretty sure it would mean Km is higher. Higher Km = lower affinity
@@laromkashy3136 with competitive, with enough substrate you can eventually knock the inhibitor out. But because this one is irreversible, the inhibitor can’t be knocked out, and so you can’t form the ES complex
I really appreciate this channel, though I would very much like to see this video redone with the MM graph all beginning at the origin, the uncompetitive inhibitor points placed according to the direction the Km and Vmax indicates they should, and perhaps a yardstick and more space between the changes in intercepts to emphasize the change in appearance of the lineweaver-burk plot's lines. Thank you for your explanation, it just took me watching the video about 10 times to put my finger on why I felt like I was understanding it here, but there being variance from other sources.
![Lineweaver-Burk plot (Enzyme Kinetics) - Vmax, Km & [S] - Biochemistry 🧪](/img/n.gif)
I'm taking a biochem class in college, I haven't learned a single thing from my lectures and you're saving me right now. I can't tell you thank you enough!
never seen someone explain such concept with so much clarity...like he was made for this
Yo, he's a doctor though.....
Yeah
Im a student from Sweden and I can only say THANKS to you!! You've saved me!
What impressed me the most with this entire video was how straight all the lines were.
😂😂
Thank you, Zack! Very comprehensively explained and yet easy to understand. This channel is one of the few that makes core concepts in biochemistry easy to follow. I’m reading Devlin’s biochemistry in sync with your videos. This channel for me is not just educational or informative which of course it is. It’s the ideal that you follow in taking such care to put top notch lectures out there that keeps me coming back nearly everyday at least in recent times. I’m planning on finishing all the lectures in a few months.
Sir ! you have an error !
you started the graph from Km ! the graph should start from 0 whatever was the type of inhibition, Km and Vmax are changing but the enzymatic reaction always start from 0. Thanks for your efforts and hardwork ❤
10k No Videos Challenge I think so there should be another line inthe graph which starts at the point 0 then goes and joins vmax line,but this line should be a little bit more curved ,so the Km will be higher and Vmax/2 will stay at the same point.(Cause vmax isnt changed)
Yes! I wanted say that but didnt know how to explain
Yup, curve always starts from zero just area under the graph increases or decrease in each Type of inhibition.
i agree,
I read the comments before watching and now I understand what you guys meant. Thanks! still a great video!
Question! Since the Km is the concentration where half the Vmax is reached, why do the lines for all the inhibitions START at Km? I feel like they should all start at zero and it should be the slope of the curves that pushes the Km to the left or right!
it might be too late to respond to your question but you're right all slopes should start a 0 because when there is no substrate there is no rate of the enzyme. It needs a substrate to operate.
Learned more in one video than an entire semester. Preciate the awesome vids!
im speechless. thank you so much for explaining everything so well
Sir i have no words to thank you, sir its very easy to understand you are amizing 😇sir iam from india from kerala state, mostly i cant never understant the foregin accent bt yr language is understandable nd easly to follow, thanks for being there to help us, 🙏😇
In class I used to sit at the end and watch your lectures😂
Thanks to you❤
This man from another planet
Superb! I was really struggling with this concept
Now I know the key is to convert the graph into Km and Vm
I feeL the graphs are incorrect since while explaining the initial graphs you made Km the starting point, instead of it being where the axis meet
I agree
initial km is for the substrate,the ones in colored ink are for inhibitors so they shift right
@@risconsiayes but why does the graph start at the km
@@risconsiano, you’re incorrect. Km is the substrate concentration which will give us half of the maximum rate of reaction (velocity) for that specific enzyme. You can’t start at Km. You start at the origin, and then shift right going for your Vmax. Then you can find the new Km in that line. But you can’t use Km as the starting point. So the graph is incorrect, I think he just didn’t notice.
@@pizzamargherita9628I agree with you mr pizza
Best video ever, the only source that made me understand everything perfectly! thanks
Simply remarkable
wow, how much the last 45 years would have been if I had you for study aide in college! relearning if so much fun !!!!
Sir if v max decreases then that red poin of y axis will b lower from the pont u mentioned
Your classes are brilliant!!
+daniela andrade coelho thank you so much for your kind words I'm so happy that we were able to help!
You are made for this job ! Thank you !
Line weaver -Burke plot begins at 12:57
Thank me later
omggggggg thanku soooo muchh you're really a very good teacher it means alot to meee thanku so muchh stay blessed ..
جزاك الله خير
Thank you so much sir
I'm speaking French I'm studying in Italy and I would work with you for helping me to buying my study. I'm able to translate ours video in Italian and French language.
😊 thank you so much
You just saved my life😊😊
You video is very very helpfull ,thank you so much ,but i have just a small suggestion ,please after the lecture take a picture of all the board then put it here 🙏🏻🙏🏻 i want to study them😊 i hope the best for you❤
you're a fantastic teacher
Dude, i have a huge confusion on that point, why are you starting the graph from the increased value of Km on x axis? shouldnt the graph still start from the zero (all three case)? because Km = [S] in half Vmax, help me please!
Salim Sikder you sir are right
Same question 🤔🤔🤔🤔🤔🤔🤔
Salim Sikder same question
Obviously hes not so good at doing graphs.... anyway still very grateful
This is actually the first blatant error I’ve witnessed after watching so many of his videos
you help medical students across the world :) greetings from Germany
I just love your vedios, highly detailed and love it how you connect different concepts.
Thanks alot. You make everything very easy to understand
Well explained. Thanks!
Thanks alot.You explained everything really well.Can you please explain y Km increases/stays the same (variation of Km) depending on nature of inhibitor?
hey zach thank you very much it helps me a lot i am happy to know you god bless you genious thank you very much
Incredible video!
You'r amazing u just made biochemistry easier for me
Thanks a lot 😍💜🤗🤗🤗🤗
Looking for more
quick question: on the graph drawn on the 9th minute 28 second
shouldn't the graph start at the origin and cross the half Vmax dotted line at the same point and normal then not make it to Vmax ?
so as to bring out the idea of no change in Km
clarify on that
Thank you 🙏🙏🙏🙏🙏🙏
I don't understand😢, if the km increases which would lead to a corresponding decrease shouldn't the graph tend towards zero given that the km is negative and the decrease once in the negative becomes bigger?
Brilliant Ninja Nerd
Great work sir
So thanks for turning something difficult in a something easy
Your lessons are amazing, a big GRAZIE from Italy
If we need to extract invertase enzymes in the lab from saccharomyces yeast and give the sample for 3 students A,B and C , they extract in the same way Under the same conditions and the same chemical student (A) get 3*Km ،Student (B) get 2*Km , Student (C) get 1*Km ,
So, who extracts the highest amount of invertase ?
It is really wonderful. Please make video explaining microscopy light and electron microscopy
hey, i don't know if I understand it wrong. But at 10.14 he draws the line for N.C.I. the Km stays the same, but the km is not the start of the line right? It's when it's 0.5Vmax right? Now in the graf the Km of normal and non competitieve inhibition isn't the same.
Could you please do a video about allosteric enzymes ?🙏🏼
Thank you for your efforts 🌹
What you don't understand about allosteric enzymes? I can explain it to you maybe
really nice lecture i understand throughly very nicely thankyou so much
very interesting and easily described lecture
what kind of cases so far that this lecture would greatly useful?
Superb sir 👌👌👌
thank you
Shouldn't the inhibitor lines start at the origin?
BRAVO 🎉
thank u so much
Thank you Sir
hello nice explanations, i have doubt that why we have to plot lineweaver bruk plot while we are getting vmax and kM from micheal -menton plot
Amazing ! Thank you so much.
Thanks once again 😊
Thanks
really useful thanks alot legend
Thank You!
Thanks again .
Thanks🙌🙌🙌🙌
Amazing
Shouldn't all of lines in the Michaelis Menten graph all start at (0,0) and the trajectory will differ depending in the different types of inhibition. The way NN drew it it looks like they start before of after normal Km which is confusing.
Where did the -1/km come from in the 2nd graph?
Great video!! i needed to slow down the video. But is because im not native english speaker.
I agree, he speaks very fast even for a native speaker. I have to pause the video a lot so I can comprehend what he says :). Keep in mind, he is speaking the language of biochemistry, which is a very dark language .. lolzz
how did we get -1/km on x axis in lineweaver-burk?
Thank you!!!
You’re welcome!
What about Irreversibile Inhibitors? You talked about them in the last video but never mentioned if the change and how they change the Vmax or Km.
Can someone help me understand it?
Because the substrate can’t bind to the enzyme, both Vmax. The substrate being unable to bind to the enzyme means no ES complex forms (affecting Vmax); the enzyme would have a much lower affinity to the enzyme (binding to the inhibitor) and I’m pretty sure it would mean Km is higher. Higher Km = lower affinity
Vmax would be lower, I meant to say
So Lower Vmax and Higher Km
Are you sure? Cus I have been reading and it seems to be exactly like a competitive inhibition
@@laromkashy3136 with competitive, with enough substrate you can eventually knock the inhibitor out. But because this one is irreversible, the inhibitor can’t be knocked out, and so you can’t form the ES complex
we dont have a line for suicide inhibition because we dont have km and vmax cuz no s was used right?
18:05 He uses the force to lift his cam up exposed.
The graphs have a bit of problem😄 but it's ok, the explanation is good and correct
km increase but what if it in 0.001 to 0.1 ? 18:04
Helpe a lot..thanks
Why is the caption is not working🤔
The t should be written in small or big
17:55
I really appreciate this channel, though I would very much like to see this video redone with the MM graph all beginning at the origin, the uncompetitive inhibitor points placed according to the direction the Km and Vmax indicates they should, and perhaps a yardstick and more space between the changes in intercepts to emphasize the change in appearance of the lineweaver-burk plot's lines. Thank you for your explanation, it just took me watching the video about 10 times to put my finger on why I felt like I was understanding it here, but there being variance from other sources.
Thanku sir
Tq
I need to send a hard question and solve it before my exam today please before 10 AM could I?
Thank youuuuu!!!!
You’re welcome!
Great great🎉🎉🎉
SOLID.
Incorrect graphical representation of enzyme inhibition. It starts from 0
I've got bad news for you, we're going to spend a lot of time together the coming year 😁😁🤭
Can you describe Kcat to me?
Vmax doesnt move
What about a mixed inhibitor?
can any one show me how we calculate enzyme activity??please!!!
You can use spectrophometer
Qasam se haya jese logon ka to moh torr dene ka Dil krta ha . Mtlb Kuch bhi ? Koi ghairat, koi sharam ?😂😂
More Videos on Lineweaver Burk plot: th-cam.com/video/wAWYIGTRXQE/w-d-xo.html
Vmax thoes change
Algún comentario en español
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