A lightweight in-browser visualization of enzyme activity vs temperature. Demonstrates:
- Increasing reaction rate with temperature up to an optimum (~37°C)
- Decline in activity due to denaturation above the optimum
- Visual distortion of enzyme active sites as temperature exceeds 37°C
- Probabilistic denaturation: enzymes remain pristine until temperature first exceeds 37°C; higher temperatures progressively denature more enzymes
- Dramatic denatured morphology (irregular spikes + red fragmented active site)
- Real-time reaction rate measurement compared to a theoretical curve
- Canvas-based particle simulation: enzymes (blue) and substrates (yellow)
- Temperature slider (0–80°C)
- Dynamic denaturation visual: active site distortion increases with temperature > 37°C
- Real-time graph: theoretical rate curve + current temperature + measured rate point
- Product counter & rolling reaction rate (average over last 10 seconds)
Just open index.html in any modern browser (no build step required).
Requires a browser with native ES Module support (any current Chrome, Firefox, Safari, Edge). If you see errors like Unexpected token 'export', make sure you didn't open the file in an extremely old browser or via a local file security restriction. Using a simple static server (example below) avoids some path issues on older setups:
python3 -m http.server 8000
# then visit http://localhost:8000- Reaction probability scales with: speed factor × temperature efficiency × remaining active-site integrity
- Speed uses a Q10-like rule (doubling ~ every 10°C) across full range (no post‑optimum slowdown) to illustrate collision theory distinctly from denaturation loss of function
- Denaturation: once temperature > 37°C, each whole-degree rise performs a probability trial for each still-native enzyme; denature severity then ramps gradually with further temperature increase
- Denatured enzymes have zero catalytic activity (they no longer contribute to product formation)
- Theoretical curve shows a deliberately steep decline after 37°C (half-life ~3°C) to visually emphasize rapid loss of functional enzymes despite continued molecular motion
- Substrate is recycled after reaction to keep counts stable
Ideas for future improvements:
- Different enzyme classes with unique optima and denaturation profiles
- Michaelis-Menten style saturation (vary substrate number)
- pH slider with combined effect matrix
- Export data (CSV) and pause/reset controls
- Replace abstract shapes with loaded SVG assets for enzymes & substrates
MIT