Lecture on Alpha Helix Structure
Introduction to Protein Structure
- Proteins have four structural levels:
- Primary structure
- Secondary structure
- Tertiary structure
- Quaternary structure
- Focus of this lecture: Secondary structures
- Types: Alpha helices, beta turns, beta pleated sheets
Focus on Alpha Helix
- Importance: Common secondary structure in proteins
- Examples: G protein-coupled receptors, transcription factors (e.g., leucine zipper motif)
Studying Alpha Helix
- X-ray Crystallography:
- Begin with protein crystallization
- Obtain diffraction pattern using X-rays
- Convert to electron density map via Fourier transformation
- Build molecular model based on the map
Alpha Helix Structure and Properties
- Discovered by Pauling and colleagues in the 1940s
- Characteristics:
- 3.6 amino acid residues per turn
- Stabilized by hydrogen bonding between I and I+4 amino acids
- Dihedral angles important, plotted using Ramachandran plot
- Right-handed helices are common
Factors Affecting Helix Stability
- Hydrogen Bonding: Crucial between I and I+4 residues
- Electrostatic Interactions:
- Repeating charged residues can cause repulsion
- Glutamate (negative charge) and lysine/arginine (positive charge)
- Helix Breakers:
- Proline: Causes structural tilt, cannot form hydrogen bonds
- Glycine: Also destabilizes the helix
- Helix Makers: Alanine, leucine, methionine
Helix Dipole and Neutralization
- Peptide bonds create a dipole with net charges
- Stabilized by opposite charges at N-terminus and C-terminus
Tools for Studying Alpha Helix
- Circular Dichroism Spectroscopy:
- Provides structural signatures of secondary structures
- Useful for identifying predominant structures in proteins
- Cryo-Electron Microscopy: Offers detailed structural insights
Summary
- Discussed alpha helix structure and stabilizing factors
- Explored techniques for studying alpha helices, including X-ray crystallography and circular dichroism spectroscopy
Feel free to reach out for more detailed studies on techniques like X-ray crystallography and circular dichroism spectroscopy.