Literature DB >> 12761183

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

Keisuke Horiuti1, Naoto Yagi, Shigeru Takemori, Maki Yamaguchi.   

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.

Entities:  

Mesh:

Substances:

Year:  2003        PMID: 12761183     DOI: 10.1093/jb/mvg025

Source DB:  PubMed          Journal:  J Biochem        ISSN: 0021-924X            Impact factor:   3.387


  2 in total

1.  Diversity of structural behavior in vertebrate conventional myosins complexed with actin.

Authors:  Hiroyuki Iwamoto; Kazuhiro Oiwa; Mihály Kovács; James R Sellers; Takuya Suzuki; Jun'ichi Wakayama; Takumi Tamura; Naoto Yagi; Tetsuro Fujisawa
Journal:  J Mol Biol       Date:  2007-03-20       Impact factor: 5.469

2.  Characterization of secophalloidin-induced force loss in cardiac myofibrils.

Authors:  Anna E Bukatina; Gary C Sieck; Kenneth B Campbell; Marek Belohlavek
Journal:  J Muscle Res Cell Motil       Date:  2009-09-11       Impact factor: 2.698

  2 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.