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Chapter 22: Problem 15

Describe the \(\beta\) -pleated structure present in some proteins.

Short Answer

Expert verified
The beta-pleated sheet is a secondary structure found in proteins. Formed by beta strands connected by hydrogen bonds, this structure can either be parallel or antiparallel. The side chains in a beta-pleated sheet extend above and below the plane of the sheet, allowing for maximum interaction and minimal steric clashes. Beta-pleated sheets are common in many proteins and contribute to their strength and flexibility.

Step by step solution

01

Definition

Start by defining the beta-pleated sheet as a secondary structure found in proteins. This structure is formed by beta strands connected laterally by two or three backbone hydrogen bonds, forming a broader pleated sheet.
02

Strand directionality

Discuss the directionality of the strands. The beta-pleated sheet can be parallel, where all component strands run in the same direction, or antiparallel, where the direction alternates.
03

Hydrogen bonding

Detail the role of hydrogen bonds. These bonds are formed between the carbonyl oxygen of one peptide bond and the hydrogen on the nitrogen atom of another peptide bond, forming a bonding network that stabilizes the sheet structure.
04

Side chain positioning

Discuss the positioning of the side chains. The side chains (R groups) of the amino acid residues in a beta-pleated sheet extend above and below the plane of the sheet, minimizing steric clashes and maximizing interactions.
05

Function and examples

Finally, mention the significance of the beta-pleated sheet structure in protein function and its occurrence in nature. Beta-pleated sheets are found in many proteins, including silk and globular proteins, and provide strength and flexibility.

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Most popular questions from this chapter

Discuss the three isomers of polypropene.

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

Discuss the characteristics of an amide group and its importance in protein structure.

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 "melting point" of a DNA molecule is the temperature at which the double- helical strand breaks apart. Suppose you are given two DNA samples. One sample contains 45 percent \(\mathrm{C}-\mathrm{G}\) base pairs while the other contains 64 percent \(\mathrm{C}\) -G base pairs. The total number of bases is the same in each sample. Which of the two samples has a higher melting point? Why?
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