Question

Examine the \(\alpha\)-helix conformation. Are amino acid side chains arranged all inside the helix, all outside the helix, or randomly?

Short answer

Answer: In the α-helix conformation of a protein, amino acid side chains are arranged perpendicularly to the helix axis and extend outward from the helix. This arrangement allows for optimal stability and interaction with other components in protein structure and function.

Step-by-step solution

Understand the α-helix conformation structure

The α-helix is a common secondary structure in proteins, characterized by a tightly coiled structure stabilized by hydrogen bonds between the backbone amide and carbonyl groups. It is formed by a specific pattern of amino acids in a polypeptide chain, in which every 3.6 residues per turn create the helical structure.

Examine the amino acid side chain arrangement in the α-helix conformation

In the α-helix conformation, the amino acid side chains are arranged perpendicularly to the helix axis and extend outward from the helix. This arrangement maximizes the stability of the helix by reducing steric clashes and allows for interactions between the side chains and other parts of the protein or solvent.

Conclude about the arrangement of side chains in the α-helix conformation

Amino acid side chains in the α-helix conformation are arranged outside the helix rather than inside or randomly. This arrangement allows for optimal stability and interaction with other components in protein structure and function.