Stabilization of the unique coiled structure of an alpha helix in a protein is mostly attributed to
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Explanation:
Two major factors stabilize the alpha helix: intrachain H-bonding and minimization of steric interference between side chains. H-bonds (colored green here) form between the oxygen of one peptide bond and the amide hydrogen four amino acids away from it along the helix.
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Stabilization of the unique coiled structure of an alpha helix in a protein is mostly attributed to Hydrogen bond from the carbonyl oxygen of one amino acid to the amino group of second amino acid.
Explanation:
- An Alpha helix is a secondary structure that gives rhe description about the arrangement of main chain of a protein in space.
- The main chain is right-handed helix with side chain pointing away from helix axis.
- An alpha helix is rod like structure tightly coiled backbone.
- The alpha helix is stablized by bonding between the Hydrogen bond from the carbonyl oxygen of one amino acid to the amino group of second amino acid.
- The bond strength is very low of single hydrogen bond however multiple hydrogen bonding gives enough stablization to the protein structure.
- It is soluble in water,enzymes,antibodies, proteins etc.
- The function of alpha helix is to do Cell block construction.
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