Energy Transport by Lattice Solitons in -Helical Proteins

Franz-Georg Mertens, Dieter Hochstrasser, and Helmut Biittner 

The fibers of striated muscles in vertebrates contain many myofibrils consisting of sar-comers. Each sarcomer consists of parallel-running thick and thin filaments. The basic mechanism for the muscle contraction consists in a sliding of the thin filaments relative to the thick ones [1]. This sliding can be described by phenomenological models consisting of a sequence of molecular processes [2, 3]. 

The thick filaments consist of myosin molecules which resemble rods with a diameter of about 40 A and a length of about 1600 A. The myosin consists of two polypeptide chains forming a double a-helical structure. At one end there are globular heads where the ATP hydrolysis takes place. 

Davydov s model has been refined or modified by several authors, which we do not discuss here because the stability of the solitons seems questionable. Both, thermal [5] and 

424 Macromolecular Systems Microscopic Interactions and Macroscopic Properties Deutsche Forschungsgemeinschaft (DFG) 

---