The best biochemistry videos on youtube, perfect for university level biochem! Thank you!
@dizisam27 жыл бұрын
I honestly don't know how i would have passed many of my exams if not for your teachings. We really appreciate everything you do! Thank You.
@TheFreshPrinceOfSaiyans5 жыл бұрын
I’m taking a 16 week Biochemistry course in 4 weeks and your videos have been super helpful. Thank you for that!
@a.v.21436 жыл бұрын
You make me appreciate science much more! Very clear and intellectual way of connecting the dots! Thanks!!
@indiramassie62375 жыл бұрын
You just save my life!!!! I’m studying for my medicine test, Step 1. You are the best teacher ever. God bless you so much!!!!!! Gracias desde el fondo de mi ♥️. I love your accent by the way.
@angkorgo6 жыл бұрын
Absolutely wonderful; I have been working on understanding these issues for about two months and in just one hour of watching these lectures things are finally becoming clear. Job well done!
@brian.israel_2 ай бұрын
LOVE your videos! Have been watching them throughout the years and your explanations help me understand complicated topics. Thank you!!
@LoganJarrell8 жыл бұрын
I will probably pass pharmacology this semester because of these videos
@Adredhead118 жыл бұрын
You are so good at explaining these topics. Thank you.
@rhastaman81185 жыл бұрын
Thank so much sir!. with respect to all teachers out there, you're the best there is. THANK YOU!!!!
@backstreetfan28873 жыл бұрын
This is the most thorough and complete video about enzyme inhibition that I have seen so far. Excellent video. One nitpicky question/concern that I have. I have also I heard of a scenario where the inhibitor binds allosterically and then changes the enzyme conformation so that the substrate does not bind. The Khan Academy video talks about that scenario and he said that it works out to be similar to competitive inhibition in practice because either the substrate is bound or the inhibitor is bound but never both (if I remember right). He calls this scenario allosteric competitive inhibition, though I don't know if anyone else refers to it that way. I checked out the wikipedia article about Mixed Inhibition and it seems that this scenario is a type of mixed inhibition. Article talks about situation where inhibitor binds allosterically and decreases apparent affinity of the enzyme for substrate, says this situation mimics competitive inhibition. So I guess it would have helped me if he talked about mixed inhibtion a bit more. In any case still a fantastic video, thanks so much for everything you do AK Lectures.
@timothytiberia8265 жыл бұрын
I would much rather pay you than these professors. You can explain something in 15 minutes that takes my professor an hour. You are a life saver!
@basmed20008 жыл бұрын
Incredibly amazing explanation. Thank you very much.
@user-lm1me6en6u2 жыл бұрын
You have the best videos! Thank you so much and keep going!
@addictivearsenal63384 жыл бұрын
how fortunate to attend your class I wish I could do it GOAT keep it up I honestly like this ak lecture channel
@rhondacorrigan50684 жыл бұрын
Thank you so much! This was such a tremendous help. Excellent explanation.
@majie_mj6 жыл бұрын
Perfect! Thx for this well explained video!
@joannejohn42187 жыл бұрын
You're so good in explaining.
@ARQ306 жыл бұрын
Perfect AK lectures and very very easy for everyone even those in pre-school.
@vav58382 жыл бұрын
These are so good, thank u so much!
@Noor-kc3yy7 жыл бұрын
it really helped thank you proffesor andrey .... perfect explination
@adamatef78257 жыл бұрын
you are amazing , please please keep going
@06davidwaterman7 жыл бұрын
Thanks man! Very helpful stuff...
@kathakalikar97015 жыл бұрын
Thk u sir for your consultation about enzyme inhibition . It helps me to clear my doubt
@nooralharbi9703 жыл бұрын
I really don’t know what to do if this channel didn’t exist .
@zeeshanshaikh45086 жыл бұрын
very clearly explained everything, thank you so much
@nataliasalamanca39464 жыл бұрын
thank you you are the best doing these explanations , before seeing your videos i was so confused
@rckildea9 жыл бұрын
excellent review!
@bilbobaggins9309 Жыл бұрын
Importantly, for competitive inhibition, the inhibitor likely has a higher affinity for the active site because the active site is shaped like the transition-state intermediate of the reaction. Many competitive inhibitors are shaped like this intermediate because the active site has a much higher affinity for the intermediate structure compared to the substrate structure.
@alexlee68595 жыл бұрын
OMG I hate my biochem textbook. Thank you for helping me out on my uni-level biochem XD
@emmanuelmaliganya Жыл бұрын
Best explanation I'm get knowledge which can help to answer different questions
@williamallotey2702 жыл бұрын
Ak always brings something you can relate to, you're a star!!! Ak😉
@rashmisingh8178 жыл бұрын
plz explain kcat/km graphically in relation to different enzymes for same substrate
@rahulgoswami35474 жыл бұрын
Thank you very much sir for to solve my problems.
@sonia_uc Жыл бұрын
thank you thank you!!!
@davidioanid13706 жыл бұрын
smartest guy on KZfaq
@loser66783 жыл бұрын
Many biological systems that utilize enzymes must be able to regulate their activity. One means of enzyme regulation involves using special agents called inhibitors (molecules or sometimes ions) that bind onto the enzymes and inhibit their activity. There are two categories of inhibitors - irreversible inhibitors and reversible inhibitors. In irreversible inhibition, the inhibitor binds very tightly to the enzyme either via covalent or non-covalent means and ultimately does not dissociate very easily, if at all, from the enzyme. Some examples of irreversible inhibitors include nerve gas, penicillin and aspirin. In reversible inhibition, the inhibitor binds onto the enzyme but can dissociate relatively easily under the proper conditions. There are four major subdivisions of reversible inhibition - competitive inhibition, uncompetitive inhibition, non-competitive inhibition and mixed inhibition. In competitive inhibition, the inhibitor resembles the substrate and binds directly to the active site. Increasing the concentration of the substrate can overcome the competitive inhibitor. In uncompetitive inhibition, the substrate must bind onto the active site before the inhibitor can bind onto the enzyme. This is because the binding of the substrate onto the enzyme creates an allosteric site on that enzyme that was not previously there. The inhibitor can now bind onto that allosteric site and create the enzyme-substrate-inhibitor complex. This complex will not go on to produce the product. Increasing the substrate concentration will not overcome an uncompetitive inhibitor. In non-competitive inhibition, the enzyme has a permanent allosteric site that the inhibitor can bind to. In addition, the inhibitor can bind to the allosteric site regardless of whether or not the substrate is bound to the active site. Increasing the substrate concentration will not effect the non-competitive inhibitor. Mixed inhibition is a more complex form of reversible inhibition in which the binding of the inhibitor essentially decreasing the affinity of the active site for the substrate and decreases the ability of the substrate to produce product molecules.
@atawahperry18526 жыл бұрын
thanks for the video it was very useful to me and my friends
@afnansalam36708 жыл бұрын
Thank you so much !
@wgdanmourad7 жыл бұрын
more than amazing thank you very much
@sanjuktaghosh88025 жыл бұрын
Hats off to you.
@zymablue Жыл бұрын
is it true if i say the substrate affinity for the enzyme's active site is higher than the inhibitor's in uncompetitive inhibition?
@xohayleyr4 жыл бұрын
For the uncompetitive inhibitor, I thought that enzymes can only undergo a conformational change when a ligand binds to its allosteric site? But you said that the substrate has to bind to its active site to make a conformational change? Was my information incorrect?
@kousarkhan67828 жыл бұрын
Hi sir, can u tell me, is molybdate competative inhibitor or non competative?
@ROCCEyg8 жыл бұрын
what would i do without you thank you very much sir ;)
@rukhaiyashaikh53604 жыл бұрын
Wel explained...👍👍
@junczhang8 жыл бұрын
thank you lots!
@alexgomez71633 жыл бұрын
Inbitors go to the enzyme bind to it shape the shape and stop production or the original functional of that enzyme
@creativefruittree34808 жыл бұрын
by non covalent did u mean even ionic bonds please help @AK LECTURES
@areebashafiq92856 жыл бұрын
Ur lectures r very good
@iqranaz71034 жыл бұрын
Sir, is it possible in competitive inhibition that 50%substrate and 50% inhibitor binds with active site of enzyme at the same time reducing the concentration of product.?
@danpuljic5 жыл бұрын
Gotta buy the full version lol
@aishasamee75166 жыл бұрын
U r great....sir
@alexgomez71633 жыл бұрын
It resembles the enzyme pattern however it's only similar not perfect so it causes that enzyme to not function
@njr1452 жыл бұрын
Thanks sir 🥰 clearly understood
@anujsirohi51647 жыл бұрын
what is the difference between poisons and inhibitors?
@axadbhatti69528 жыл бұрын
nice work
@henrychinex82786 жыл бұрын
we love yo vedios man keep it up #makanyanyachibaa
@soulrain67 жыл бұрын
Thank you🌸🌸🌸
@Textbook0005 жыл бұрын
I think homeboy is great👍🏼👌🏻👊🏽
@aninvisiblepiper7 жыл бұрын
I wish i found these videos sooner :/
@jakemacisaac78992 жыл бұрын
fucking love this guy
@muyabinmgaza8 жыл бұрын
thank you
@gjzztrrettmmggrrertzhgyena49504 жыл бұрын
Thsnk yuo ...very much....🌺🌺🌺🌺
@kamelkachin78487 жыл бұрын
Thank you so so soooooooooooooooo much
@gideonmuchina92424 жыл бұрын
I actually understand
@LS-gh8sz8 жыл бұрын
excellent explanation- however why is uncompetitive inhibition a sub tyoe of reversible inhibition if the inhibition cannot be overcome by increasing the conc of the substrate, wouldnt that mean its irreversible
@codyo66645 жыл бұрын
The difference is in the binding. For the irreversible once the e+ I is made it no longer can dissociate. For uncompetitive the inhibitor can leave the allosteric set making the enzyme usable once more. Does that help?
@gloriaadeyemi98023 жыл бұрын
Am kinda confused pls, is allosteric inhibition the same as uncompetitive inhibition?
@arusawaseem67373 жыл бұрын
Allosteric inhibition is binding to the allosteric site, whilst uncompetitive inhibition involves binding to the enzyme-substrate complex
@MrPridizzle6 жыл бұрын
I don't always drink.... but when I do.... I prefer XX...
@patricemulemwa50282 жыл бұрын
Wow
@alexgomez71633 жыл бұрын
Penicillin helps production
@aya4532 Жыл бұрын
❤❤❤❤❤❤
@HelloWorld-vt8bg8 жыл бұрын
How we can stop a non competitive inhibitor ??? i need it pleaaaase answer
@mitcheldijkhof69828 жыл бұрын
+ali wassim it depends, some are irreversible others reversible. Cyanide is reversible non-competitive. it binds to ferric ion of cytochrome oxidase, but it binds better to the ferric ion of methemoglobin, which has low levels in the body. administering sodium nitrate causes extra methemoglobin production. causing cyanide to form cyanomethemoglobine.
@HelloWorld-vt8bg8 жыл бұрын
+Mitchel Dijkhof Thanx , most of non competitive are reversible , so i need more details of how we can stop them. Please help me i need that answer...
@AK-di4rv7 жыл бұрын
Starts at 8:20
@Pcarnevaaa Жыл бұрын
What that means is Should be on a shirt
@zerakhu5 жыл бұрын
Mirin
@user-xl6hf1gw6d5 жыл бұрын
Always save me
@rosheenkamal1564 жыл бұрын
i love u
@mschoplos8 жыл бұрын
textbook answer lol
@VideoMakesMeHappy Жыл бұрын
3 ESI looking sus
@nouralshihaby74764 жыл бұрын
Man I miss your accent Indian voices hurt my ears
@Serajis6 жыл бұрын
You talk too much!
@issi29075 жыл бұрын
How do u think he's supposed to make people understand without talking
@emanzaidi88486 ай бұрын
then read a book duh
@williamallotey2702 жыл бұрын
Ak always brings something you can relate to, you're a star!!! Ak😉