# Module 2: The Weaver

> Learn how amino acids form secondary structures — alpha helices, beta sheets, and loops.

Local Structure

Learn how amino acids form secondary structures — alpha helices, beta sheets, and loops.

- Explain the i → i+4 backbone hydrogen bonding that holds an alpha helix together
- Distinguish parallel from antiparallel beta sheets by their hydrogen bond geometry
- Identify the structural roles of loops, turns and the residues that favour them
- Predict where proline and glycine will break regular secondary structure
- Read a Ramachandran plot and explain which backbone geometries are forbidden and why
- Predict secondary structure from sequence alone using residue propensities

## Links

- [Introduction](https://proteindesign.academy/module/2/intro)
- [2.1 The Alpha Helix](https://proteindesign.academy/module/2/1)
- [2.2 Beta Sheets](https://proteindesign.academy/module/2/2)
- [2.3 Loops, Turns & the Unsung Heroes](https://proteindesign.academy/module/2/3)
- [2.4 Helix Breakers & Structural Disruptors](https://proteindesign.academy/module/2/4)
- [2.5 Backbone Geometry: The Ramachandran Map](https://proteindesign.academy/module/2/5)
- [2.integration Secondary Structure Prediction](https://proteindesign.academy/module/2/integration)
- [The Pattern Master](https://proteindesign.academy/module/2/capstone)
- [Start Here](https://proteindesign.academy/start-here)
- [Tools & Papers](https://proteindesign.academy/tools-and-papers)
- [Continuing Practice](https://proteindesign.academy/continuing-practice)