Internal dynamics of F-actin and myosin S1 studied by quasi elastic neutron scattering

Matsuo, Tatsuhito; Arata, Toshiaki*; Oda, Toshiro*; Fujiwara, Satoru

The dynamics of F-actin and myosin S1 were studied by quasi-elastic neutron scattering (QENS). QENS measurements were conducted on D2O solution samples of F-actin and S1 at 300 K using AMATERAS in J-PARC. It was found that while the correlation time of atomic motions of S1 was similar to that of other proteins studied so far, that of F-actin was shorter than S1. Furthermore, the fraction of immobile atoms were found to be larger for S1 than F-actin. These results suggest that F-actin is more flexible than other proteins including S1.

Language	:	Japanese
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Meeting title	:	生体運動合同班会議2015
Held date	:	2015/01
Location (city)	:	東京
Location (country)	:	日本
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Keywords	:	中性子散乱; タンパク質; ダイナミクス
Research Facility	:	J-PARC物質・生命科学実験施設
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Registration No. : BB20142826
JAEA Abstracts No. :
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