An x-ray diffraction study on the ADP-induced conformational change in skeletal muscle myosin

J Biochem. 2003 Feb;133(2):207-10. doi: 10.1093/jb/mvg025.

Abstract

Effects of ADP on the conformation of myosin cross-bridges were studied in x-ray diffraction experiments on single skinned fibers of frog skeletal muscle by photorelease of ADP from caged-ADP. The experiments were performed at the third-generation synchrotron radiation facility SPring-8 with a time resolution of 5 ms. The intensity of the third-order meridional reflection from myosin filaments (at 1/14.4 nm(-1)) increased promptly after the ADP release with a time constant smaller than 5 ms, which was similar to that of tension decline. The results show that ADP binding induces a conformational change of myosin in skeletal muscle fibers.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Diphosphate / analogs & derivatives*
  • Adenosine Diphosphate / chemistry*
  • Adenosine Diphosphate / radiation effects
  • Animals
  • Light
  • Muscle Contraction
  • Muscle Fibers, Skeletal / chemistry
  • Muscle Fibers, Skeletal / physiology
  • Muscle, Skeletal / chemistry*
  • Myosins / chemistry*
  • Nitrobenzenes / radiation effects
  • Phase Transition
  • Protein Conformation
  • Rana catesbeiana
  • Time Factors
  • X-Ray Diffraction*

Substances

  • Nitrobenzenes
  • P(2)-(1-(2-nitrophenyl)ethyl) ADP
  • Adenosine Diphosphate
  • Myosins