# Module 1: The Building Blocks

> Master the 20 amino acids — their chemistry, physical properties, and roles in protein structure.

Amino Acid Properties

Master the 20 amino acids — their chemistry, physical properties, and roles in protein structure.

- Classify the twenty amino acids by the properties that decide where they sit in a fold
- Predict whether a residue belongs in the buried core or on the solvent-exposed surface
- Explain the hydrophobic effect as the dominant driving force behind folding
- Reason about the four interaction types that hold a fold together: burial, electrostatics, packing, and aromatic stacking
- Recognise why proline, glycine and cysteine behave unlike any other residue
- Design a short peptide that satisfies charge, core, salt-bridge and stacking constraints at once

## Links

- [Introduction](https://proteindesign.academy/module/1/intro)
- [1.1 The Hydrophobic Effect](https://proteindesign.academy/module/1/1)
- [1.2 Electrostatics & Salt Bridges](https://proteindesign.academy/module/1/2)
- [1.3 Size & Shape: The Packing Game](https://proteindesign.academy/module/1/3)
- [1.4 The Special Characters](https://proteindesign.academy/module/1/4)
- [1.5 Aromatic Interactions](https://proteindesign.academy/module/1/5)
- [The Peptide Engineer](https://proteindesign.academy/module/1/capstone)
- [Start Here](https://proteindesign.academy/start-here)
- [Tools & Papers](https://proteindesign.academy/tools-and-papers)
- [Continuing Practice](https://proteindesign.academy/continuing-practice)
