Question

Hydrogen bonds between peptide backbone components form a distinct helical structure of

Secondary
primary
Tertiary
quaternary
Secondary structure is characterized by which one of the following types of interactions?
hydrogen bonding within the N and C of peptide backbone
a covalent bond between two amino acids
ionic bonding between an acidic R group and a basic R group
hydrogen bonding between R groups of amino acids

Answer 1

proteins are known as the alpha helix. The hydrogen bonds play a crucial role in stabilizing the secondary structure of proteins. In an alpha helix, the backbone components, which include the carbonyl oxygen and the amide hydrogen, participate in hydrogen bonding interactions.

The hydrogen bonding occurs between the carbonyl oxygen of one amino acid residue and the amide hydrogen of an amino acid residue four positions down the sequence. This pattern of hydrogen bonding repeats along the length of the helix, resulting in a tightly coiled structure. The hydrogen bonds form between the electronegative oxygen atom and the partially positively charged hydrogen atom, creating a stable interaction.

The hydrogen bonds in the alpha helix contribute to its stability and rigidity. They help to maintain the helical shape by holding the backbone components in place. The hydrogen bonding pattern also allows for efficient packing of the amino acid side chains along the helix axis, further stabilizing the structure.

The alpha helix is a common structural motif found in proteins, and its formation is critical for their overall folding and function. It provides structural stability and allows for specific interactions with other molecules, such as in protein-protein or protein-DNA interactions.

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