Ontology highlight
ABSTRACT:
SUBMITTER: Matsuo T
PROVIDER: S-EPMC4629667 | biostudies-literature | 2013
REPOSITORIES: biostudies-literature
Matsuo Tatsuhito T Arata Toshiaki T Oda Toshiro T Fujiwara Satoru S
Biophysics (Nagoya-shi, Japan) 20130723
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 chymotryptic S1 was evaluated to be 41.3±1.1 Å for SAXS, 40.1±3.0 Å for SANS in H2O, and 37.8±0.8 Å for SANS in D2O, respectively. The values of the cross-sectional radius of gyration of F-actin were 25.4±0.03 Å for SAXS, 23.4±2.4 Å for SANS i ...[more]