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Journal Articles

Electrostatic potential of nucleotide-free protein is sufficient for discrimination between adenine and guanine-specific binding sites

Basu, G.*; Sivanesan, D.*; Kawabata, Takeshi*; Go, Nobuhiro

Journal of Molecular Biology, 342(3), p.1053 - 1066, 2004/09

https://doi.org/10.1016/j.jmb.2004.07.047

Times Cited Count：23 Percentile：35.53(Biochemistry & Molecular Biology)

no abstracts in English

Oral presentation

Determination of hydrogen positions of photoactive yellow protein

Yamaguchi, Shigeo*; Kamikubo, Hironari*; Kurihara, Kazuo; Shimizu, Tetsuya*; Yamazaki, Yoichi*; Kuroki, Ryota; Niimura, Nobuo*; Kataoka, Mikio*

no journal, ,

Oral presentation

Dynamic and static structure factor for Staphylococcal Nuclease measured by neutron scattering

Endo, Hitoshi; Tominaga, Taiki; Takata, Shinichi; Matsumoto, Atsushi; Iwase, Hiroki*; Kamikubo, Hironari*; Kataoka, Mikio

no journal, ,

The dynamic and static structure factors for Staphylococcal Nuclease (SNase), which is a nucleolytic enzyme derived from Staphylococcus aureus, were evaluated by neutron spin echo (NSE)and small-angle neutron scattering (SANS) experiments. The SANS experiment was performed with TAIKAN (BL15) time-of-flight diffractometer at J-PARC/MLF, and we could obtain the static structure factors with wide Q range (0.2 Q[1/ 2). The NSE measurement was performed with IN15 spectrometer at ILL. Grenoble, which enabled us to obtain intermediate scattering functions over 200 nanoseconds. The effects of hydration and internal motions were considered.