PROTEIN FOLDING SIMULATION

An amino-acid chain has so many possible conformations that testing them one by one would outlast the universe, yet a real protein folds in a few thousandths of a second, because the hydrophobic core collapses and drags the rest of the chain with it. The extended chain first coils into α-helices and β-sheets, and those elements pack into a compact three-dimensional shape: the more deeply the core is buried, the lower the energy and the more stable the fold. Too much heat unravels the fold into denaturation, while misfolding lets chains stick together into amyloid fibres.

▸ 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
About Protein Folding

An amino-acid chain has so many possible conformations that testing them one by one would outlast the universe, yet a real protein folds in a few thousandths of a second, because the hydrophobic core collapses and drags the rest of the chain with it. The extended chain first coils into α-helices and β-sheets, and those elements pack into a compact three-dimensional shape: the more deeply the core is buried, the lower the energy and the more stable the fold. Too much heat unravels the fold into denaturation, while misfolding lets chains stick together into amyloid fibres.

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