Steered molecular dynamics and mechanical functions of proteins

Atomic force microscopy of single molecules, steered molecular dynamics and the theory of stochastic processes have established a new field that inves tigates mechanical functions of proteins, such as ligand-receptor binding/u nbinding and elasticity of muscle proteins during stretching. The combinati on of these methods yields information on the energy landscape that control s mechanical function and on the force-bearing components of proteins, as w ell as on the underlying physical mechanisms.