| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
Biophys J, December 1999, p. 3197-3207, Vol. 77, No. 6
and
*LLS-IFAE, Universitat Aut-noma de Barcelona, E-08193
Bellaterra, Barcelona, Spain; #Department of Physics and
Astronomy, University of Leicester, Leicester LE1 7RH, United Kingdom;
§Department of Physics, Oliver Lodge Laboratory,
University of Liverpool, Liverpool L69 3BX, United Kingdom;
¶Open University Research Unit, Boars Hill, Oxford
OX1 5HR, United Kingdom; Daresbury Laboratory,
Warrington WA4 4AD, United Kingdom; and **ESRF, 220, F-38043 Grenoble
Cedex, France
When isometrically contracting muscles are subjected to a
quick release followed by a shortening ramp of appropriate speed (Vo), tension decays from its value at the isometric
plateau (Po) to <0.05 Po with the same time
course as the quick part of the release; thereafter, tension remains at
a negligible level for the duration of the shortening ramp. X-ray
diffraction data obtained under these conditions provide evidence that
1) at Vo very few heads form an actomyosin complex, while
the number of heads doing so at Po is significant; 2)
relative to rest the actin filament at Vo is ~0.12%
shorter and more twisted, while it is ~0.3% longer and less twisted
at Po; and 3) the myosin heads attaching to actin during
force development do so against a thin filament compliance of at least
0.646 ± 0.046% nm per Po.
Biophys J, December 1999, p. 3197-3207, Vol. 77, No. 6
© 1999 by the Biophysical Society 0006-3495/99/12/3197/11 $2.00
This article has been cited by other articles:
 |
|
 |
|
  M. Linari, E. Brunello, M. Reconditi, Y.-B. Sun, P. Panine, T. Narayanan, G. Piazzesi, V. Lombardi, and M. Irving The structural basis of the increase in isometric force production with temperature in frog skeletal muscle J. Physiol., September 1, 2005; 567(2): 459 - 469. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 N. Yagi, H. Iwamoto, J. Wakayama, and K. Inoue Structural Changes of Actin-Bound Myosin Heads after a Quick Length Change in Frog Skeletal Muscle Biophys. J., August 1, 2005; 89(2): 1150 - 1164. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
A. K. Tsaturyan, N. Koubassova, M. A. Ferenczi, T. Narayanan, M. Roessle, and S. Y. Bershitsky Strong Binding of Myosin Heads Stretches and Twists the Actin Helix Biophys. J., March 1, 2005; 88(3): 1902 - 1910. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
J. Borejdo, A. Shepard, D. Dumka, I. Akopova, J. Talent, A. Malka, and T. P. Burghardt Changes in Orientation of Actin during Contraction of Muscle Biophys. J., April 1, 2004; 86(4): 2308 - 2317. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
H. Iwamoto, J.'i. Wakayama, T. Fujisawa, and N. Yagi Static and Dynamic X-Ray Diffraction Recordings from Living Mammalian and Amphibian Skeletal Muscles Biophys. J., October 1, 2003; 85(4): 2492 - 2506. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
T. Yamada, Y. Takezawa, H. Iwamoto, S. Suzuki, and K. Wakabayashi Rigor-Force Producing Cross-Bridges in Skeletal Muscle Fibers Activated by a Substoichiometric Amount of ATP Biophys. J., September 1, 2003; 85(3): 1741 - 1753. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
X. Liu and G. H. Pollack Mechanics of F-Actin Characterized with Microfabricated Cantilevers Biophys. J., November 1, 2002; 83(5): 2705 - 2715. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
S. Y. Bershitsky and A. K. Tsaturyan The elementary force generation process probed by temperature and length perturbations in muscle fibres from the rabbit J. Physiol., May 1, 2002; 540(3): 971 - 988. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
