Muscle contraction and polymer-gel phase transitions

Artificial muscles typically contrast by a phase-transition. Muscle is thought to contract by a different mechanism - a filament-sliding mechanism in which one set of filaments is driven past another by the action of cyclically rotating cross-bridges. The concept is much like the mechanism of rowing. The evidence, however, is equally consistent with a mechanism in which the filaments themselves contract, much like the condensation of polymers during a phase-transition. Muscle contains three principal polymer types organized neatly into a characteristic framework All three polymers can shorten. The contributions of each filament may be designed to confer versatility, as well as sped and strength, on this biological machine. The principles of natural contraction may be useful in establishing optimal design principles for artificial muscles.

[1]  C. Schutt,et al.  Actin as the generator of tension during muscle contraction. , 1992, Proceedings of the National Academy of Sciences of the United States of America.

[2]  H E Huxley,et al.  The low-angle x-ray diagram of vertebrate striated muscle and its behaviour during contraction and rigor. , 1967, Journal of molecular biology.

[3]  N. Yagi,et al.  Cross-bridge movements during a slow length change of active muscle. , 1984, Biophysical journal.

[4]  T. Tameyasu,et al.  Stepwise dynamics of connecting filaments measured in single myofibrillar sarcomeres. , 1998, Biophysical journal.

[5]  G H Pollack,et al.  Actin-filament motion in the in vitro motility assay has a periodic component. , 1997, Cell motility and the cytoskeleton.

[6]  M. Rief,et al.  Reversible unfolding of individual titin immunoglobulin domains by AFM. , 1997, Science.

[7]  G. Pollack,et al.  Thick filaments of striated muscle are laterally interconnected. , 1988, Journal of ultrastructure and molecular structure research.

[8]  R. M. Simmons,et al.  Elasticity and unfolding of single molecules of the giant muscle protein titin , 1997, Nature.

[9]  H. E. Keurs,et al.  Sarcomere shortening in striated muscle occurs in stepwise fashion , 1977, Nature.

[10]  P. Janmey,et al.  Cooperativity in F-actin: binding of gelsolin at the barbed end affects structure and dynamics of the whole filament. , 1996, Journal of molecular biology.

[11]  R. Goody,et al.  Time-resolved cryo-electron microscopic study of the dissociation of actomyosin induced by photolysis of photolabile nucleotides. , 1991, Journal of molecular biology.

[12]  Stepwise shortening in unstimulated frog skeletal muscle fibres. , 1985, The Journal of physiology.