Alpha helix || secondary structure of protein 

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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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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

sure

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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.

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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

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It's from Lehninger's Biochem text book

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Lehninger/ Voet

No it's a amide bond ( covalent)

Then which is hydrogen bond in protein structure?

I am really sorry for the inconvenience

@@animatedbiologywitharpan its ok , i hope you add translation at your next videos