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Difference in hydration structures between F-actin and myosin subfragment-1 detected by small-angle X-ray and neutron scattering

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

Hydration structures around F-actin and myosin subfragment-1 (S1), which play central roles as counterparts in muscle contraction, were investigated by small-angle X-ray scattering (SAXS) and small-angle neutron scattering (SANS). The radius of gyration of S1 was evaluated to be 41.3 $$pm$$ 1.1 ${AA}$ for SAXS, 40.1 $$pm$$ 3.0 ${AA}$ for SANS in H$$_{2}$$O, and 37.8 $$pm$$ 0.8 ${AA}$ for SANS in D$$_{2}$$O, respectively. The values of the cross-sectional radius of gyration of F-actin were 25.4 $$pm$$ 0.03 ${AA}$ for SAXS, 23.4 $$pm$$ 2.4 ${AA}$ for SANS in H$$_{2}$$O, and 22.6 $$pm$$ 0.6 ${AA}$ for SANS in D$$_{2}$$O, respectively. Analysis showed that the hydration shell of S1 has the average density 10-15% higher than bulk water, being the typical hydration shell, while the hydration shell of F-actin has the average density more than 19% higher than bulk water, indicating that F-actin has a denser, unusual hydration structure. The results indicate a difference in the hydration structures around F-actin and S1.



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