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State difference between the alpha-helix...

State difference between the `alpha`-helix and `beta`-pleated sheet configuration.

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(i) `alpha`-helix configuration. In this type of structure of polypertides chains undergo hydrogen bonding, in which the NH and CO group of the same chain are involved in the H-bonding. This type of hydrogen bonding coils the peptide chain to form a right handed helix called `alpha`-helix. Myosin and keratin are examples of `alpha`-helix structure.
(ii) `beta`-pleated sheet configuration. In this type of structure protein chains are stretched out and assume pleated sheet structure. Each chain is held to the two neighbouring chains by hydrogen bonds. Silk fibroin has pleated sheet structure.
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Proteins are found to have two different types of secondary structures viz. alpha -helix and beta -pleated sheet structure. alpha -helix structure of protein is stabilised by :