Its been 4 years. I dont know what college u went, but this comment represents me now. I was overwhelmed for understand nothing in class. Thanks my lecturer recommend this vid afterwards.
Omg these lectures are flawless I literally wanna cry from happiness. it’s been 8 years since they have been published but the best lectures I have ever watched
These Videos were post/published almost 2 years ago and am here enjoying every part of em...Biochemistry seemed so tough but now i feel like all i needed was to take a glimpse at these videos and thats was it...Thank you AK LECTURE your knowledge via is really more than helpful..
Thanks so much for all your lectures!!!!you should come to our university!!!you make biochemistry so easy and i appreciate your hard work and the way you structure your lectures in a way that everyone can understand!!!!!!!keep up the good work!!!
Am grateful for these free services.Biochemistry is now very easy for me. God bless and I hope to make a reasonable donation of this good course someday.Thanks and more strength
I feel like you just saved me so many hours of studying the long poorly worded book to understand what you just taught me in 10 minutes (thanks to 1.5 speed haha). You are awesome!!!!!
You go so much more in depth with these topics than my teacher, that I dont have to keep constantly asking myself "why does this happen" or "we seem a bit short on notes." Thanks for this :)
i listen ur lecture it help me a lot in my exams ur way of teactng is awesome ...ii enjoy ur lecture it deeply penetrate in my mind thnx AK LECTUREs :)
love you lectures so much. you make things simple and easy to understand. i was wondering what references you use for this topic? hope i get a reply from you :)
The efforts and the way of teaching is so frickin sick, prof! I have accepted the fact that most of the teachers have knowledge but they cannot convey it properly Except some who are god gifted like you❤
h ak million times of sorry! i didn't let you know after my exam and i saw your message just now! of course it did well. and just because of you:) i recommend your videos to every of my friends and will keep recommending... billions of thanks again...
A question, if the formation of a-helices and b-sheets depend exclusively on the H-bonds of the polypeptide backbone, and not on the side chains (which are variable), what does determine if an a-helix or b-sheet will take place? Because the N-H and C=O of the backbone will always be the same! You are a great teacher, thanks!
The amino acid residues within the polypeptide chain determine what conformation will occur. Proline, glycine, and charges amino residues disrupt the alpha helix so if they're found in a protein, that section will likely be a beta turn. Small hydrophobic residues like alanine and leucine, on the other hand, are perfect for forming alpha helices.
Hello professor..I am Marchela-a chemistry student. I would like to ask some questions. 1. How to know the end of alpha -helix or beta sheet structure in protein? 2. What is the impact of having short loop and long loop in secondary protein and in which kind of protein that has long or short loop? Thank you for you responbility
Your videos are really good. I understand everything better, when you explain it, even though I am from Austria and a native german speaker. You should teach at my University of Pharmacy :-)
I'm confused, question: "The peptide bonds have a double bond character" but I noticed all the drawings of the C-N bond appear as a single bond, is this "character" you're speaking of indicatory of a resonance occuring between the C=O double bond and the C-N bond? Thus causing it to have another double bond character as to not freely rotate? Tyvm! Excellent...really excellent lectures btw. Liked & subscribed.
Is there a list of amino acid sequences organized into the two main categories: 1. Alpha helix 2. Beta-pleated sheet? I recently made a program that randomly generates an amino acid sequence. The program stops when a stop codon is generated. That is, there's a 3/64 the program will stop after each amino acid is generated. However, I'm unable to find the necessary information to create a program of perfect information for the secondary structure.
No se como hace, pero hace que in tema que parecia inabordable, parezca fácil. Creia que si no tenía una computadora de última generación, jamás lo iba a poder entender... Congratulations!!!
One doubt: in carbohydrates(starch, glycogen) it was the alpha linkage which helps in compactness(twist and turn) and in proteins beta turn. My question is why the name is beta turn not alpha turn (in proteins) and is alpha turn exist?, if not then why?
I could not understand how the parallel beta sheet amino acid residues of polypeptide sheet form two hydrogen bonds with the amino acid of the opposite chain. Please elucidate further Waiting for an answer :D
Is the beta sheet consist of more than one peptide/polypeptide chain and beta turns connected them to result in a one polypeptide chain? or it is one polypeptide chain and the side that turns it called beta turns?
Good lecture bro, i have a question. can you show right handed and left handed cross over connection in parallel beta sheet. i have a doubt in understanding why the images in books look opposite ( i mean the right handed one looks left hand to me, I think i am interpreting those images wrongly)
Could anyone please help me understand how a proteins secondary structure is determined between alpha, beta, omega etc? I know it’s defined by the pattern of hydrogen bonds between the amino hydrogen and carboxyl oxygen in the peptide backbone but is this truly spontaneous?? If we aren’t accounting for the R group then shouldn’t they all fold into the same secondary structure?
Good point. Prior to this video, I understood the *R* sidechains played a major role in determining the secondary structure. But you're right, he barely mentioned them. Odd.
Can you tell me why there is a decimal number of amino acid residues 3.6 in alpha helix and how can be an amino acid residue be a decimal number and not a whole number?
Isn't the hydrogen bond in the a-helix also like an n+3 case rather than a "four units ahead" one? Sorry that line just got me confused but I completely get the point 😂
![COLOMBIA vs. CHILE [4-0] | RESUMEN | ELIMINATORIAS SUDAMERICANAS | FECHA 10](http://i.ytimg.com/vi/TDjN4W3yy1k/mqdefault.jpg)
"and what that means is..."
so beautiful.
thank you.
the amount of respect I have for just being able to draw out alpha helix, with detail and legibility. its beyond me
For non-English speakers, what could be a synonym for rad-like structure?
this is so helpful. thank u
Your videos are sick bro. Making this biochem significantly easier... summing 2 hour conversations into 14 mins. Thanks
Its been 4 years. I dont know what college u went, but this comment represents me now. I was overwhelmed for understand nothing in class. Thanks my lecturer recommend this vid afterwards.
@@vanessamumu1968 its been another year. This video = still relevant
I have been a loyal lover of the lectures, 3 years now
still relevant, and the best..
Still
Omg these lectures are flawless I literally wanna cry from happiness. it’s been 8 years since they have been published but the best lectures I have ever watched
These Videos were post/published almost 2 years ago and am here enjoying every part of em...Biochemistry seemed so tough but now i feel like all i needed was to take a glimpse at these videos and thats was it...Thank you AK LECTURE your knowledge via is really more than helpful..
Some more additional information: β-turns often consist of Glycine which provides flexibility and Proline, which provides steric constraints.
You're excellent, 4 years back I used to learn modern physics from ak lectures
Now as a medical student learning biochem
You are so versatile
6 years ago they were posted and still they are mesmerising.....you are god gifted mateeeee❤
You r one of the best teacher for me to come across . A great job and thus a great apreciation
Bt where r u now ?
No more uploads !?
"wow, this is a H, not a N" 😂😂😂
13:26
Thanks so much for all your lectures!!!!you should come to our university!!!you make biochemistry so easy and i appreciate your hard work and the way you structure your lectures in a way that everyone can understand!!!!!!!keep up the good work!!!
I used to hate this subject, but wow, you just made me fall in love with proteins.
Thank you so much
this video was published when i was in 5th grade, and now, im a 1st yr college student who you just saved. tysmm
Am grateful for these free services.Biochemistry is now very easy for me. God bless and I hope to make a reasonable donation of this good course someday.Thanks and more strength
Sir, Thank you so much!! I have my biochemistry exam tomorrow and I rely on your videos to do well on it.
I feel like you just saved me so many hours of studying the long poorly worded book to understand what you just taught me in 10 minutes (thanks to 1.5 speed haha). You are awesome!!!!!
2022 and you taught me more than my prof in university. thank u so much !!
You go so much more in depth with these topics than my teacher, that I dont have to keep constantly asking myself "why does this happen" or "we seem a bit short on notes."
Thanks for this :)
i listen ur lecture it help me a lot in my exams ur way of teactng is awesome ...ii enjoy ur lecture it deeply penetrate in my mind thnx AK LECTUREs :)
The best videos I have ever watched. Thank you for these wonderful explanations. Could you please explain omega loop as well?
Kind Regards
love you lectures so much. you make things simple and easy to understand. i was wondering what references you use for this topic? hope i get a reply from you :)
Dianne Galang good in lippincott biochem
Thank you a lot ...the way you explain even a new born baby can even understand
The efforts and the way of teaching is so frickin sick, prof!
I have accepted the fact that most of the teachers have knowledge but they cannot convey it properly
Except some who are god gifted like you❤
13:26 that wow described my whole process of learning from this video 😂 Thank you soo much 💕
Nicely explained men . You have explained the basic compositions of structure . It's good for me
i Don't know how i express my greatfullness. thanks a lot sir.
Helpful stuff. But you didn't talk about omega loops :(
Very well explained sir. Clear explanation. You are a true inspiration....
i've my phD proficiency exam tomorrow and i'was prepared with your amazing videos. wish me luck:)
semiramis yilmaz good luck! let me know how it turns out!
+semiramis yilmaz how did it go ?
The world will never know"
Mona :P :*(
h ak million times of sorry! i didn't let you know after my exam and i saw your message just now! of course it did well. and just because of you:) i recommend your videos to every of my friends and will keep recommending... billions of thanks again...
you explain in such a nice way that it makes me
so easy to understand
Your explanation unbelievable!!
A question, if the formation of a-helices and b-sheets depend exclusively on the H-bonds of the polypeptide backbone, and not on the side chains (which are variable), what does determine if an a-helix or b-sheet will take place? Because the N-H and C=O of the backbone will always be the same!
You are a great teacher, thanks!
The amino acid residues within the polypeptide chain determine what conformation will occur. Proline, glycine, and charges amino residues disrupt the alpha helix so if they're found in a protein, that section will likely be a beta turn. Small hydrophobic residues like alanine and leucine, on the other hand, are perfect for forming alpha helices.
excellent review videos for MCAT biochem, thank you
just22ish thats wonderful! :-) best of luck with the exam! definitely a mental marathon.
That's one hell of a drawing. Huge props for that Helix
Thank you so much. Made more sense than my lecturer. I'm a med student.......
I swear this finally makes sense! thanks so much!!!!
Hello professor..I am Marchela-a chemistry student. I would like to ask some questions.
1. How to know the end of alpha -helix or beta sheet structure in protein?
2. What is the impact of having short loop and long loop in secondary protein and in which kind of protein that has long or short loop?
Thank you for you responbility
Your videos are really good. I understand everything better, when you explain it, even though I am from Austria and a native german speaker. You should teach at my University of Pharmacy :-)
you are awesome, so easy to understand
I'm confused, question: "The peptide bonds have a double bond character" but I noticed all the drawings of the C-N bond appear as a single bond, is this "character" you're speaking of indicatory of a resonance occuring between the C=O double bond and the C-N bond? Thus causing it to have another double bond character as to not freely rotate?
Tyvm! Excellent...really excellent lectures btw. Liked & subscribed.
Give that man a cookie
clear explanation starting from basics thank you !
The notes on the board are so crisp I didn't even need to watch the whole video to understand!
Extraordinary teaching 🤩
you are an excellent teacher
Your videos are absolutely amazing !! thank you so much for all of them
great! but i just want to know what is the difference between (loop region - beta turns - disordered region( ??
Is there a list of amino acid sequences organized into the two main categories: 1. Alpha helix 2. Beta-pleated sheet? I recently made a program that randomly generates an amino acid sequence. The program stops when a stop codon is generated. That is, there's a 3/64 the program will stop after each amino acid is generated. However, I'm unable to find the necessary information to create a program of perfect information for the secondary structure.
Literally u r awesome sir🤩🤩
May god bless u always 🙌🙌🙌
U explain each and every concept very smoothly 🤍🤍
The R groups on the anti parallel lower chain have their chirality reversed (wedges should be dashes, and vice versa).
sir your lectures are amazing.
I also request you to make a video on Ramachandran plot.
Your explanation is something beyoooonnnnddd!!!!
Thanks so much for making everything easier to understand!
seriously sir....ur lectures are awesome
u r also osm
BC
A left-handed α-helix results in steric hindrance between the side chains and the C=O groups from the amide/peptide bonds.
very good video thanks for the amount of detail and effort!
No se como hace, pero hace que in tema que parecia inabordable, parezca fácil.
Creia que si no tenía una computadora de última generación, jamás lo iba a poder entender...
Congratulations!!!
fantastic
You haven't explained 4th type of secondary structure
Please, which protein secondary structure is more stable as a single stand-alone element, alpha or b-sheet?
You r doing a great job
You make it too easy! thank you thank you and one more thank you
One doubt: in carbohydrates(starch, glycogen) it was the alpha linkage which helps in compactness(twist and turn) and in proteins beta turn.
My question is why the name is beta turn not alpha turn (in proteins) and is alpha turn exist?, if not then why?
kudos!!! Thank you so much for explaining everything in such detail
والله كفو, احسن من د نبيل تبعنا
I could not understand how the parallel beta sheet amino acid residues of polypeptide sheet form two hydrogen bonds with the amino acid of the opposite chain. Please elucidate further
Waiting for an answer :D
thank you for the lecture, make me understand easily.. by the way, can u explain the omega loop structure too?
Is the beta sheet consist of more than one peptide/polypeptide chain and beta turns connected them to result in a one polypeptide chain? or it is one polypeptide chain and the side that turns it called beta turns?
Jumana S both can be the case
Thank you🫡 شكرا
Awesome lecture 👌
Спасибо! Довольно доступно все объяснено)
You are amazing sir,hats-off
Beta paleted structure is composed by alpha helix or directly?
Good lecture bro, i have a question. can you show right handed and left handed cross over connection in parallel beta sheet. i have a doubt in understanding why the images in books look opposite ( i mean the right handed one looks left hand to me, I think i am interpreting those images wrongly)
Amazing lectures!
Could anyone please help me understand how a proteins secondary structure is determined between alpha, beta, omega etc? I know it’s defined by the pattern of hydrogen bonds between the amino hydrogen and carboxyl oxygen in the peptide backbone but is this truly spontaneous?? If we aren’t accounting for the R group then shouldn’t they all fold into the same secondary structure?
Good point. Prior to this video, I understood the *R* sidechains played a major role in determining the secondary structure. But you're right, he barely mentioned them. Odd.
Do you have a video on super secondary, and phi, psi, omega bondage?
Super secondary are motifs..go for Garet
beautiful explanation!
you are so good like really good lmaooo this is insane! im taking my money back from my teacher because i only learn from you
Thank you for the greattt explanation..
amazing lecture
Thank you sir,it was so helpful for me 🤗
Amazing thank you thank you from the bottom of my brain!
Can you tell me why there is a decimal number of amino acid residues 3.6 in alpha helix and how can be an amino acid residue be a decimal number and not a whole number?
Just awesome . Thank you a lot..
sir you are a great keep it up
Isn't the hydrogen bond in the a-helix also like an n+3 case rather than a "four units ahead" one? Sorry that line just got me confused but I completely get the point 😂
you are just woww evenn... keep it up, do a series on organic chemistry maybe
Alpha helix is a round like structure that contain the back bone been inside of the helix and the side chain group of what
thank you a lot.. its really helpful....
How much percentage of beta sheets in beta keratin and flavodoxine??
Reallly helpful,Thanks
good work thanks
love your videos!
Four units ahead meaning the first unit and the fifth unit?
Thank you so much, you're a lifesaver!
you're welcome!
8:55 to 9:06 why is C=O referred to Hydrogen group, isn't it supposed to be carbonyl
I mean ... he explains better than my professor ...
Why does an alpha helix be formed?
Thank you so much Sir ❤️