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Chapter 27: Problem 54

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

Short Answer

Expert verified
Answer: In the α-helix conformation, amino acid side chains are arranged on the outside of the helix.

Step by step solution

01

Understanding the α-helix conformation

The α-helix is a common secondary structure in proteins, formed by hydrogen bonding between the backbone atoms of amino acids within a protein chain. This pattern results in a right-handed helix structure, with the carbonyl (C=O) group of each amino acid residue forming a hydrogen bond with the amide (NH) group of another amino acid situated about 3.6 residues away along the polypeptide chain.
02

Arrangement of the amino acid side chains

In the α-helix structure, the amino acid side chains (R groups) are not involved in the hydrogen bonding, and they protrude outwards from the helix. This means that the side chains are not situated within the helix itself but externally, projecting to the outside of the helix.
03

Conclusion

In the α-helix conformation, amino acid side chains are arranged on the outside of the helix. They are not located inside the helix or arranged randomly. This specific arrangement allows for the stabilization of the α-helix structure through hydrogen bonding and provides space for potential interactions between side chains and other components of the protein or its surroundings.

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Most popular questions from this chapter

If a protein contains four different SH groups, how many different disulfide bonds are possible if only a single disulfide bond is formed? How many different disulfides are possible if two disulfide bonds are formed?

A tetradecapeptide (14 amino acid residues) gives the following peptide fragments on partial hydrolysis. From this information, deduce the primary structure of this polypeptide. Fragments are grouped according to size. $$ \begin{array}{ll} \hline \text { Pentapeptide Fragments } & \text { Tetrapeptide Fragments } \\ \hline \text { Phe-Val-Asn-Gln-His } & \text { Gln-His-Leu-Gys } \\ \text { His-Leu-Cys-Gly-Ser } & \text { His-Leu-Val-Glu } \\ \text { Gly-Ser-His-Leu-Val } & \text { Leu-Val-Glu-Ala } \\ \hline \end{array} $$

Define the term zwitterion.

Why are Glu and Asp often referred to as acidic amino acids?

The BOC-protecting group may be added by treatment of an amino acid with di- tert-butyl dicarbonate as shown in the following reaction sequence. Propose a mechanism to account for formation of these products.
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