The stiffness of the crossbridge is a function of the intrinsic protein osmotic pressure generated by the crossbridge itself
- 3 June 1996
- journal article
- Published by Wiley in FEBS Letters
- Vol. 387 (2-3) , 101-104
- https://doi.org/10.1016/0014-5793(96)00481-4
Abstract
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 × 105dynes/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 × 107 and 3.3 × 108 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.Keywords
This publication has 18 references indexed in Scilit:
- Osmotic properties of the calcium-regulated actin filamentBiochemistry, 1995
- Actin May Contribute to the Power Stroke in the Binary Actomyosin SystemBiochemical and Biophysical Research Communications, 1994
- Osmotic Stress Is the Main Determinant of the Diameter of the Actin FilamentBiochemical and Biophysical Research Communications, 1993
- Atomic model of the actin filamentNature, 1990
- Molecular packing in profilin: Actin crystals and its implicationsJournal of Molecular Biology, 1989
- Osmoelastic coupling in biological structures: formation of parallel bundles of actin filaments in a crystalline-like structure caused by osmotic stressBiochemistry, 1989
- Nonideality of volume flows and phase transitions of F-actin solutions in response to osmotic stressBiophysical Journal, 1987
- [29] Osmotic stress for the direct measurement of intermolecular forcesPublished by Elsevier ,1986
- Polarized fluorescence from ε-ADP incorporated into F-actin in a myosin-free single fiber: Conformation of F-actin and hanges induced in it by heavy meromyosinJournal of Molecular Biology, 1978
- The structure of F-actin and of actin filaments isolated from muscleJournal of Molecular Biology, 1963