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Chapter 25: Problem 15

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

Short Answer

Expert verified
The \(\beta\)-pleated sheet is a secondary structure in proteins where the polypeptide chain folds back and forth on itself, creating a 'pleated' sheet-like structure. It is stabilized by hydrogen bonds between the carbonyl oxygen of one amino acid and the amide hydrogen of another. The folding could be parallel or antiparallel, depending on the orientations of the chains. The structure provides significant strength and stability to the protein structure by maximizing hydrogen bonds.

Step by step solution

01

Definition and Formation

The \(\beta\)-pleated sheet is a secondary structure found in proteins. It is formed when the polypeptide chain folds back and forth on itself, creating a pleated, sheet-like structure. This folding could be parallel (where chains run in the same N to C orientation) or antiparallel (where chains run in opposite directions).
02

Description of Structure

The 'pleats' in the \(\beta\)-pleated sheet are the result of the amino acid side chains, which extend above and below the plane of the sheet. The sheet itself is stabilized by hydrogen bonds between the carbonyl oxygen of one amino acid and the amide hydrogen of another, aligning in a regular pattern.
03

Significance in Proteins

The \(\beta\)-pleated sheet conformation is particularly stable and allows parts of the protein to align closely together, maximizing the number of hydrogen bonds and therefore the strength and stability of the overall protein structure. This configuration provides structural integrity to many proteins, including fibrous structural proteins and globular proteins.

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