3D Protein Structure Visual Laboratory

Press Start Lesson to watch one amino-acid chain organize into a working protein.

ΔGfold = Gfolded − GunfoldedPrimary chain · 28 residues · peptide backbone intact

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Protein controls

Structural level

Temperature37 °C

pH7.0

Hydrophobic effect100%

Reducing agent breaks S—S

ΔGfold = −18.0 kJ/mol · folded state favored

Peptide backboneSide-chain chemistryStabilizing contacts

hydrophobicpolarchargedcysteine

Speed1×

Zoom100%

Tap a residue, peptide bond, or stabilizing contact for a molecular close-up.

LanguageNarrator

Lesson speed1×

Seven chapters · twenty-one synchronized visual beats

Embedded, amplified audio plays through the tab and can be captured by an external tab recorder. No microphone is needed.

ΔGfold = Gfolded − Gunfolded; negative ΔGfold favors folding

Relate amino-acid sequence to primary, secondary, tertiary, and quaternary structure.
Distinguish peptide bonds from hydrogen bonds, ionic attractions, hydrophobic packing, and disulfide bridges.
Predict how heat, extreme pH, and reducing agents alter protein shape.
Connect three-dimensional structure with biological function.

Use the ten-page touch whiteboard for sequences, structural sketches, interactions, equations, and uploaded images.

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