ニュース

2017年06月02日 掲載 (Published 06/02/2017)


「Biophysics and Physicobiology」にKotomi Shibata et al. “Mutations in the SH1 helix alter the thermal properties of myosin II”を掲載

日本生物物理学会欧文誌[Biophysics and Physicobiology]に以下の論文が新規掲載されました。

Kotomi Shibata, Tsubasa Koyama, Shohei Inde, Sosuke Iwai, Shigeru Chaen “Mutations in the SH1 helix alter the thermal properties of myosin II”

【Significance】
Mutations in the myosin II SH1 helix influence the thermal properties

Myosin II SH1 helix is a joint that links the converter subdomain to the rest of the myosin motor domain. In this study, we introduced the E683K or R686C point mutation into the SH1 helix in Dictyostelium myosin II, and found that these mutations decreased both the thermal stability of myosin II and the activation energy of a rate-limiting process involved in actin movement, suggesting that the SH1 helix is a key structural element that determines the flexibility and thermal properties of the myosin motor.


Biophysics and Physicobiology, Vol.14, pp. 67-73

URL:https://www.jstage.jst.go.jp/article/biophysico/14/0/14_67/_article