HomeBiophysicsTitin Domain Unfolding 2D: AFM Force Spectroscopy

Titin Domain Unfolding: AFM Force Spectroscopy (2D)

Pull a 2D chain of titin Ig-domains with a virtual AFM cantilever and watch the classic sawtooth force-extension curve emerge as each folded domain unfolds under load, modelled with the worm-like chain (Marko-Siggia) and Bell's force-dependent unfolding kinetics — pan and zoom the chain view yourself.

Biophysics2DAdvanced60 FPS📱 Mobile-adapted⇄ 3D version
2d-physics-ext-topic-65 ↗ Open standalone

This simulator models a single molecule of titin — the giant elastic protein of the muscle sarcomere — as it is stretched by a virtual atomic-force-microscope cantilever, exactly as in the single-molecule pulling experiments that first revealed how titin generates passive muscle tension. A 2D chain of folded immunoglobulin (Ig) domains is pulled at a controllable speed; force builds along a worm-like-chain curve until one domain's force-dependent unfolding rate (Bell's model) makes it snap open, adding ~25 nm of new contour length and dropping the force before the cycle repeats — producing the classic sawtooth force-extension trace plotted live beneath the pannable, zoomable chain view.

⚙ Under the hood

Pull a 2D chain of titin Ig-domains with a virtual AFM cantilever and watch the classic sawtooth force-extension curve emerge as each folded domain unfolds under load, modelled with the worm-like chain (Marko-Siggia) and Bell's force-dependent unfolding kinetics — pan and zoom the chain view yourself.

biophysicstitinprotein unfoldingAFMforce spectroscopymuscle mechanics

2D · HTML5 Canvas 2D · 60 FPS target · runs fully client-side, no install

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