Biochemistry | Michaelis Menten Equation
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- เผยแพร่เมื่อ 25 เม.ย. 2017
- Official Ninja Nerd Website: ninjanerd.org
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In this lecture Professor Zach Murphy will present on the Michaelis Menten Equation. We hope you enjoy this lecture and be sure to support us below!
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Watched this video for my undergraduate biochem class and got an A+ in the class. Watching again to study for the MCAT. You’re a great teacher brother
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Could you please enable subtitles on this video and the other biochemistry videos? I'm deaf and would really like to watch.
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I tried reading this on my own and it felt like my head was being pounded in. Thank you so much, I understood it perfectly!
Really helpful. When my professor tried to derive it, everyone was confused lol kudos to you and thank you :)
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It’s just like the movies we ignore the random equations in the background
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Watching.
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Km does not equal 1/2Vmax
- units for KM is concentration (moles)
- units for 1/2Vmax is concentration/per time
Km equals "concentration [S] at which Vo=1/Vmax"
How can v max ever be half of initial velocity pls exaplin
Enjoyed learning it. Thank you
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20:35
theorising here any experts correct me
going back to the definition of Km = K-1 + K2 / K1
where Km essentially is the rate of dissociation over association
a low Km = high affinity
a low Km means that either the rate of association is higher and/or the rate of dissociation is lower, so more ES is formed high affinity
high Km = low affinity
vice versa, rate of dissociation is higher while association is lower
in the context of affinity referring to how much substrate an enzyme can take on, I'm guessing that k2 is higher rather than the effects of k-1 being higher or K1 being smaller (though i thought that affinity would refer to how fast K1 would be)
so low Km means higher affinity, K2 is lower, less substrate can be taken on as ES complexes take longer to form into E + P
while high Km means lower affinity, K2 is higher, more substrate can be taken on as ES complexes are freed up quicker
Thank you so much. Great job 👍
Thank you a lot. You made me understood the Michaelis Menten equation with ease
Thankyou for your efforts sir these videos are very very helpful
Great video, little bit different from my book but really helped me understand the topic.
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The best video for Michael menten equation all over the internet 😶🌫️
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So helpful. Thanks :) Will you also do The eyring-polyani equation??
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very good sir , please create video on different plots in enzymology
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Super helpful! However, how would we find the Vmax without using the Lineweaver equation or plot?
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Thanks for this great lecture❤ , I wanna ask : do you recommend a biochemistry book which is well-organized and straightforward to the information
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i think there are few mistakes.. one of which is mathematical around min 9:15 when u divided the equation by k1 - you didn't divided the subtraction as well..
Could you please add subtitles, for people from other countries who don’t know english very well(and also for me)
Thanks a lot...u save my day
+Aditi Barman You’re welcome! Happy studies!
Hello! This video was very helpful, thank you so much!! I had one question though, in my textbook they refer to kcat, which measures the # of substrate molecules turned over/converted to product, per enzyme per molecule per second. They give the following equation: Vmax=kcat[E]. Going of off this lecture I can see that we used k2 instead, but I'm confused as to why they used the reactant concentration, because what I took from this video was that at Vmax we only have the [ES] for the total amount of our enzyme. I can see them using Vmax=kcat[ES], but I think I am probably misunderstanding something. If you could please explain it would be greatly appreciated! Thank again (:
greetings sir . we thanks you for your teaching. please I have a question to ask.
please can u make a video on the differences between the Michaelis menten approach and the Brigg Haldane approach of enzyme kinetics. I can't really see a difference btw this two approaches
Thank u so much
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Ty!