Answer:
theres not photo my guy
You didn't put a photo.
b. A plastic cup
c. A television set
d. A wool sweater
Answer:
In the α helix structure, there is a hydrogen bonding between oxygen atom in a carbonyl of one amino acid and the hydrogen atom of the amino group that is situated four residues farther along the polypeptide chain
Explanation:
The common secondary structure of protein are: α helix and β pleated sheet
α helix is a rod like structure.It is a right handed coil of amino acid residue on a polypeptide chain, which may be 4 units or 40 units long. The coil is held together by hydrogen bond between oxygen atom in a carbonyl of one amino acid and the hydrogen atom of the amino group that is situated four residues farther along the polypeptide chain. This means that every complete turn of the helix is only 3.6 residues.
In an alpha helix, hydrogen bonds are formed between the carbonyl oxygen of one amino acid and the hydrogen attached to the nitrogen atom of another amino acid that is four residues away in the same polypeptide chain. This results in the characteristic spiral structure of an alpha helix.
In an alpha helix, a type of secondary structure in proteins, there is a specific pattern of hydrogen bonding that helps maintain its spiral shape. The hydrogen bond is formed between the carbonyl oxygen (C=O) of one amino acid and the hydrogen (H) attached to the nitrogen atom (N-H) of another amino acid that is four residues away in the same polypeptide chain. This repeated pattern of hydrogen bonding results in the characteristic spiral structure of the alpha helix. In terms of polypeptide numbering, if the amino acid at position n in the chain forms a hydrogen bond, then it does so with the amino acid at position n+4. This bonding pattern, along with the characteristics of the specific amino acids involved, contributes to the overall stability and function of the protein.
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j: (Sipping his tea). What about your family?