Alpha helix || secondary structure of protein
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- čas přidán 21. 09. 2020
- This video talks about the alpha helix structure of proteins.The α helix, a common structural motif of proteins, consists of a right-handed helix with a repeat length of 3.6 amino acid residues per helical turn. The α helix is stabilized by hydrogen bonds between an amide hydrogen of one amino acid and a carbonyl oxygen four amino acids away.
I am first year MBBS student and I have watched your many videos ...they always make the things very simple and easy to understand 👍🏻👍🏻 keep it up and thank u for amazing content
I will give you a detailed answer of your question soon when I am near my laptop. But anyway please share my videos with your mbbs friends
Have you passed mbbs test?If passed how many marks you got
9:22 ....I have question ..as u have said the alpha helix ends are slightly polar so they are neutralized by negatively charged group on N terminal end and positively charged group on C terminal end so I have to ask do alpha helices always end with *Lys* or *Arg* in C terminal end? I mean lysine or arginine is used to neutralize it to attain stability so would there always be Lys or Arg at that end?
Amazing!!! A lot better explained than my uni professors
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Awesome explanation and the animations looks so cool :) thanks bro
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Great sir 🔥🔥🔥
Have a quiz tomorrow, this helped me so much. Thank you kind sir!
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so cool thank you
Don’t forget to share with your classmates
@@animatedbiologywitharpan i sure will thank you ♥️
Hi!
is there a specific order for amino acids to be able to form an alpha helix? for exempel i had an exam question where they asked “ will this order of amino acid sequences form an alphab helix?” and the right answer were “no because every third amino acid is positive charged”
Different amino-acid sequences have different propensities for forming α-helical structure. Methionine, alanine, leucine, glutamate, and lysine uncharged ("MALEK" in the amino-acid 1-letter codes) all have especially high helix-forming propensities, whereas proline and glycine have poor helix-forming propensities. Proline either breaks or kinks a helix, both because it cannot donate an amide hydrogen bond (having no amide hydrogen), and also because its sidechain interferes sterically with the backbone of the preceding turn - inside a helix, this forces a bend of about 30° in the helix's axis. However, proline is often seen as the first residue of a helix, it is presumed due to its structural rigidity. At the other extreme, glycine also tends to disrupt helices because its high conformational flexibility makes it entropically expensive to adopt the relatively constrained α-helical structure.
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Awesome explanation Sir, 😊
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around 8:02
- for Alanine you put the beta-alanine structure (you meant to put alpha-alanine)
- the structures of methionine and leucine are inversed
Where is table 6.1 from? Like what textbook
It's from Lehninger's Biochem text book
Thank you!
Can you make a video on maxam Gilbert sequencing? Please
I need some time
@@animatedbiologywitharpan it's alright, you're the best study channel bro.
@@tunerd1921 please share with your friends
Awesome... I've never watched such an informative and clearly understanding video I have exam tomorrow and this helps me alot thanks 😊
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So, alpha helix structure contain one polypeptide chain??
not necessary ...we cant imagine alpha helix as a isolated entity ....in a protein there could be a long peptide chain and some part might take a conformation of alpha helix and some other part may take a conformation of beta pleated sheet....keep on watching this video series....things would be clear
@@animatedbiologywitharpan thank you. This is helpful :)
very very helpful, thank you
Please help me by sharing with your class mates
Sir can we have videos on loops nd tertiary structure?
Soon those videos would be uploaded
I used this for last min uni prep
Worked out great
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brother it's my request to u that please make 11 and 12 ncert based biology animation vedio and form all chapter's playlist bcz these vedios help a lot to neet aspirants included me
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Check out all my playlist.....you might find interesting things
kamal💯
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Nice👍👍
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just a small concern on the material of this video. H-bonding between alpha C and N in the backbone isn't it between 1st C and 4th N (n+3 not n+4).
No I am totally confident about the material .please refer to the following point.
in alpha 3.6 (13 ) helix every mainchain C=O and N-H group is hydrogen-bonded to a peptide bond 4 residues away (ie O(i) to N(i+4)). This gives a very regular, stable arrangement.
In contrast to 3.6(13 ) helix the 3(10) helix has a different pattern.Here the main chain hydrogen bonds are between residues separated by three residues along the chain (ie O(i) to N(i+3)).
Literature support :www.pnas.org/content/pnas/100/20/11207.full.pdf
check out the original feb 1960 nature paper as well
www.sci-hub.ren/www.nature.com/articles/185422a0
Wow.... Thanks
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@@animatedbiologywitharpan sure Sir
can you make vedio on structure of fibrinogen
sure
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Awesome
please share among your friends
@@animatedbiologywitharpan yeah.Nice work.I really like your animations
Tq sir
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Thanks
Could you please help me by sharing my contents with your friends group/ college group. I put huge efforts in making these videos but unfortunately not a lot of people are watching this.
Could you please help me by sharing my contents with your friends group/ college group. I put huge efforts in making these videos but unfortunately not a lot of people are watching this.
Dada Tumi Kon book follow korecho ba korechile etar jonno?
Lehninger/ Voet
Sir can u explain about major and minor groove of DNA
Yes very soon there would be videos on that
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@@animatedbiologywitharpan yes am already shared among my frnds sir
Thank you sir. Clear and concise!
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Please make lecture video on Riboswitches
Ok it would be uploaded soon
@@animatedbiologywitharpan thank you sir🙂
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could not understand
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IFAS biochemistry ka playlist me upka vidio dekha?
Thanks for informing......I don't know how that happened....I am not linked with them
@@animatedbiologywitharpan Ha ha, actually upka vidio slides bahot famous hai😂😂
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As a gd player I would add one to the start of the name
can we say peptide bond is hydrogen bond ?
No it's a amide bond ( covalent)
Then which is hydrogen bond in protein structure?
Why there is no translation 😕
I am really sorry for the inconvenience
@@animatedbiologywitharpan its ok , i hope you add translation at your next videos
HBB gene 🧬 147❤ honey 👌🦚🐝