Key result
At a physiological protein osmotic pressure of 1.8 x 10(5) dynes/cm2, the elastic moduli by bending of the monomer in F-actin and myosin subfragment-1 decorated F-actin are 6.5 X 10(7) and 3.3 X 10(8) dynes/cm2.
This basic science model demonstrates that the elastic modulus by bending of the monomer is directly related to the intrinsic protein osmotic pressure of the system.
Establishes osmotic pressure dependence of actin elasticity in vitro; leaves open relevance to cardiac sarcomere mechanics.
A model is presented that makes it possible to determine the stiffness of the crossbridge from protein osmotic stress experiments. The model was elaborated while studying the osmotic properties of F-actin and of myosin subfragment-1 F-actin. These studies showed that the elastic modulus by bending of the monomer is directly related to the intrinsic protein osmotic pressure of the system. At a protein osmotic pressure of 1.8 x 10(5) dynes/cm2, the physiological protein osmotic pressure of frog skeletal muscle, it was found that the elastic moduli by bending of the monomer in F-actin and in the myosin subfragment-1 decorated F-actin are 6.5 X 10(7) and 3.3 X 10(8) dynes/cm2, respectively. The value of the elastic modulus by bending of the monomer in the myosin subfragment-1 decorated F-actin compares favorably with the values of the elastic modulus by stretching determined in skeletal muscle fibres.
No takes yet. Share an insight, caveat, or question.
Grazi et al. (1996) studied this question. At a physiological protein osmotic pressure of 1.8 x 10(5) dynes/cm2, the elastic moduli by bending of the monomer in F-actin and myosin subfragment-1 decorated F-actin are 6.5 X 10(7) and 3.3 X 10(8) dynes/cm2.
Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context: