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Journal Articles

Conformational ensemble of a multidomain protein explored by Gd$$^{3+}$$ electron paramagnetic resonance

Saio, Tomohide*; Hiramatsu, Soya*; Asada, Mizue*; Nakagawa, Hiroshi; Shimizu, Kazumi*; Kumeta, Hiroyuki*; Nakamura, Toshikazu*; Ishimori, Koichiro*

Biophysical Journal, 120(15), p.2943 - 2951, 2021/08

 Times Cited Count:1 Percentile:7.79(Biophysics)

A rigid double-arm lanthanide tag was utilized in electron paramagnetic resonance spectroscopy to measure the distance between two specific points on a protein, and conformational states and distribution of a multi-domain protein enzyme MurD was investigated. Although the previous crystallographic and NMR studies have reported the three distinct conformational states of MurD, our data unveiled that the protein exists in much more variety of conformational states in the absence of the ligand. Given the fact that MurD is one of the potent drug target for infectious diseases, the finding in this study will provide important structural basis for drug development.

Journal Articles

Formation of advanced tokamak plasmas without the use of an ohmic-heating solenoid

Shiraiwa, Shunichi*; Ide, Shunsuke; Ito, Satoshi*; Mitarai, Osamu*; Naito, Osamu; Ozeki, Takahisa; Sakamoto, Yoshiteru; Suzuki, Takahiro; Takase, Yuichi*; Tanaka, Shigetoshi*; et al.

Physical Review Letters, 92(3), p.035001_1 - 035001_4, 2004/01

 Times Cited Count:48 Percentile:82.9(Physics, Multidisciplinary)

no abstracts in English

Oral presentation

Construction of a BNCT facility using an 8MeV high power proton linac in Ibaraki

Kobayashi, Hitoshi*; Kurihara, Toshikazu*; Matsumoto, Hiroshi*; Yoshioka, Masakazu*; Matsumoto, Noriyuki*; Kumada, Hiroaki*; Matsumura, Akira*; Sakurai, Hideyuki*; Hiraga, Fujio*; Kiyanagi, Yoshiaki*; et al.

no journal, , 

no abstracts in English

Oral presentation

Application of a lanthanide tag for evaluation of conformational states of a multidomain protein

Saio, Tomohide*; Nakagawa, Hiroshi; Hiramatsu, Soya*; Asada, Mizue*; Kawamukai, Honoka*; Nakamura, Toshikazu*; Ishimori, Koichiro*

no journal, , 

Despite their importance in function, the conformational states and changes of proteins are often poorly understood mainly because of the lack of an efficient tool. MurD, a 47-kDa three-domain protein enzyme responsible for peptidoglycan biosynthesis, is one of those proteins whose conformational states and changes during its catalytic cycle are not well understood. We exploited multiple biophysical methods including nuclear magnetic resonance, electron paramagnetic resonance, small-angle scattering, and molecular dynamics simulation to demonstrate evaluation of the conformational states and distribution of MurD. The integrated use of these methods can be an efficient strategy to evaluate the conformational states and distribution of proteins in solution.

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