Beta-sheet

A fundamental secondary protein structure consisting of aligned polypeptide strands stabilized by hydrogen bonds, forming pleated sheet-like configurations essential for protein architecture and function.

Beta-sheet

Beta-sheets (β-sheets) represent one of the most important secondary structure elements in proteins, discovered by William Astbury in the 1930s and later refined by Linus Pauling and Robert Corey. These structures form when multiple segments of a polypeptide chain align parallel or antiparallel to each other, creating a distinctive pleated pattern.

Structure and Formation

Basic Architecture

  • Composed of beta-strands (β-strands)
  • Connected by hydrogen bonds between:
    • C=O groups of one strand
    • N-H groups of adjacent strand
  • Forms a pleated appearance due to tetrahedral geometry of amino acids

Types of Beta-sheets

  1. Parallel β-sheets

    • Strands run in same direction (N→C terminus)
    • Slightly less stable configuration
  2. Antiparallel β-sheets

    • Strands run in opposite directions
    • More common and typically more stable

Stabilizing Forces

The stability of beta-sheets depends on several factors:

Biological Significance

Functional Roles

Disease Relevance

Beta-sheets play crucial roles in various pathological conditions:

Common Protein Examples

Beta-sheets are found in numerous important proteins:

Analysis Methods

Scientists study beta-sheets using various techniques:

Engineering Applications

Understanding beta-sheets has led to various applications:

Relationship to Other Structures

Beta-sheets often work in concert with other structural elements:

Understanding beta-sheets remains crucial for:

  • Predicting protein structures
  • Designing new proteins
  • Developing treatments for protein-related diseases
  • Advancing biotechnology applications