In α – helix the bonding occurs between oxygen of carbonyl group of one amino acid and hydrogen of amino group of
Question
In α – helix the bonding occurs between oxygen of carbonyl group of one amino acid and hydrogen of amino group of
Solution 1
In an α-helix structure, the bonding occurs between the oxygen atom of the carbonyl group of one amino acid and the hydrogen atom of the amino group of another amino acid. Here are the steps:
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The α-helix is a common secondary structure in proteins. It is a right-handed coiled or spiral conformation, in which every backbone N-H group donates a hydrogen bond to the backbone C=O group of the amino acid located three or four residues earlier along the protein sequence.
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The carbonyl (C=O) group of one amino acid is involved in this bonding. The carbonyl group is a super functional group present in all amino acids, peptides, and proteins. The carbonyl group consists of a carbon atom double-bonded to an oxygen atom.
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The amino group (-NH2) of another amino acid, specifically the one located three or four residues earlier in the sequence, is also involved in the bonding. The amino group consists of a nitrogen atom attached by single bonds to hydrogen atoms.
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A hydrogen bond forms between the oxygen atom of the carbonyl group of one amino acid and the hydrogen atom of the amino group of the other amino acid. This hydrogen bond is what holds the spiral α-helix structure together.
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The specific pattern of hydrogen bonding produces a helix with the repeating pattern of backbone atoms, which is the characteristic of the α-helix structure.
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This process repeats along the length of the polypeptide chain, causing it to take on a coiled, spring-like shape. This is the α-helix structure, one of the most common structures found in proteins.
Solution 2
In an α-helix structure of proteins, the bonding occurs between the oxygen atom of the carbonyl group of one amino acid and the hydrogen atom of the amino group of another amino acid. This is a specific type of bonding known as hydrogen bonding.
Here are the steps:
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The α-helix structure is one of the most common secondary structures in proteins. It is a right-handed coiled or spiral arrangement of the protein chain.
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This structure is stabilized by hydrogen bonds, which are interactions between a hydrogen atom attached to a highly electronegative atom (like oxygen or nitrogen) and another electronegative atom.
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In the case of the α-helix, the hydrogen bonds occur between the oxygen atom of the carbonyl group (C=O) of one amino acid and the hydrogen atom of the amino group (N-H) of another amino acid.
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Specifically, the hydrogen bond forms between the carbonyl of one amino acid and the amino group of the fourth amino acid down the chain. This pattern of bonding pulls the chain into a helical structure.
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These hydrogen bonds are relatively weak, but the cumulative effect of many hydrogen bonds along the length of the α-helix contributes significantly to the stability of the structure.
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