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Chapter 22: Problem 14

What is the \(\alpha\) -helical structure in proteins?

Short Answer

Expert verified
The 伪-helical structure in proteins is a right-handed coiled or spiral configuration of amino acids stabilized by hydrogen bonds. It is a common structural element in proteins, contributing to protein stability, flexibility, and functionality.

Step by step solution

01

Definition

The alpha helix (伪-helix) is one of the primary ways that proteins can form their three-dimensional structure. It is a right-handed coiled or spiral configuration, in which all the backbone N-H groups (donor) of amino acids are hydrogen bonded to the backbone C=O groups of the amino acid situated three or four residues earlier along the protein sequence (acceptor).
02

Characteristics

A protein's alpha-helical structure has several defining characteristics. Each turn of the helix involves 3.6 amino acid residues, with an axial rise per residue of 1.5脜 and a pitch (length of one complete turn along the helix axis) of 5.4脜. The alpha-helical structure is stabilized by hydrogen bonds. These bonds form between the hydrogen of the -NH group of an amino acid and the oxygen of the carbonyl group of another amino acid, typically four residues away.
03

Role in Proteins

The alpha helix is a vital structural component in a vast array of proteins. The alpha helix structures can vary in length and they play a crucial role in establishing the characteristics and functionality of the proteins. For example, they are prevalent in haemoglobin and keratin. The functionality of the protein, its stability, flexibility and the dynamics of the protein are determined by the alpha-helical content in the protein structure.

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Most popular questions from this chapter

Describe the formation of polystyrene.

What kind of intermolecular forces are responsible for the aggregation of hemoglobin molecules that leads to sickle-cell anemia?

When a nonapeptide (containing nine amino acid residues) isolated from rat brains was hydrolyzed, it gave the following smaller peptides as identifiable products: Gly-Ala-Phe, Ala-Leu-Val, Gly-Ala-Leu, Phe-Glu-His, and His-Gly-Ala. Reconstruct the amino acid sequence in the nonapeptide, giving your reasons. (Remember the convention for writing peptides.)

The folding of a polypeptide chain depends not only on its amino acid sequence but also on the nature of the solvent. Discuss the types of interactions that might occur between water molecules and the amino acid residues of the polypeptide chain. Which groups would be exposed on the exterior of the protein in contact with water and which groups would be buried in the interior of the protein?

When deoxyhemoglobin crystals are exposed to oxygen, they shatter. On the other hand, deoxymyoglobin crystals are unaffected by oxygen. Explain. (Myoglobin is made up of only one of the four subunits, or polypeptide chains, in hemoglobin.)
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