Protein Folding Challenge
Welcome to the Protein Folding Challenge! In this game, you'll learn about how proteins fold into their functional 3D structures based on the properties of their amino acids.
How to Play:
1. Click on amino acids to fold them into a stable structure.
2. Hydrophobic amino acids (yellow) prefer to be together in the core.
3. Hydrophilic amino acids (blue) prefer to be on the outside.
4. Polar amino acids (red) can form bonds with other polar amino acids.
5. Try to create a stable protein with the highest possible score!
Stability Score: 0
Level: 1
The Science Behind Protein Folding
Proteins are essential macromolecules that perform a vast array of functions within living organisms. The function of a protein is determined by its three-dimensional structure, which is in turn determined by its amino acid sequence.
Protein folding is driven by various forces including:
- Hydrophobic interactions: Non-polar amino acids tend to cluster in the core of the protein, away from water.
- Hydrogen bonding: Forms between polar amino acids, stabilizing the structure.
- Electrostatic interactions: Attractions between oppositely charged amino acids.
- Van der Waals forces: Weak attractions between atoms in close proximity.
Understanding protein folding is crucial for many areas of biology and medicine, including drug design and understanding diseases caused by protein misfolding, such as Alzheimer's and Parkinson's.