PROTEIN FOLDING SIMULATION

▸ Loading the polypeptide chain (amino-acid sequence)…
▸ Assigning R side-chain properties (hydrophobic/hydrophilic, charge)
▸ Building backbone hydrogen bonds → α-helix / β-sheet
▸ Calibrating the free-energy funnel
▸ Loading chaperones & misfolding module (amyloid)
▸ Ready — Online. ✅
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⌂ Cells & Genetics

Simulation room Protein folding

Protein Folding · shape = function
Online
sequence · folding funnel · lock-and-key
Folding level & energy
🧬 Sequence → structure
Amino acids—
Structure level—
Hydrophobic core—
Energy (ΔG)—
Status—
Viewing—
Note
Sequence determines structure (Anfinsen): the folding information already resides in the amino-acid chain. Hydrophobichydrophobic groups bury into the core away from water, hydrophilic groups face out → the 3D fold. Misfolding → amyloid aggregation (Alzheimer’s, prions).
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Pick a folding stage (primary → secondary → tertiary · chaperone · misfolding · function) · drag "Folding progress" / "Temperature" · click a concept for details
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Folding funnel — free energy drops as it folds stability (ΔG↓)foldedhydrophobic core