SANS simulation of aggregated protein in aqueous solution

Masaaki Sugiyama, Kei Hamada, Koichi Kato, Eiji Kurimoto, Kenta Okamoto, Yukio Morimoto, Susumu Ikeda, Sachio Naito, Michihiko Furusaka, Keiji Itoh, Kazuhiro Mori, Toshiharu Fukunaga

Research output: Contribution to journalArticlepeer-review

9 Citations (Scopus)


Small-angle neutron scattering (SANS) of aggregated protein in an aqueous solution is simulated based on the crystallographic data of the protein. After obtaining the crystallographic data of the target protein, hydrogen atoms are added to the data and then some hydrogen atoms are replaced with deuterium atoms. The structure models are made with this data and then their gyration radii and SANS intensities are calculated. Compared the calculated SANS data with the experimental one, the most probable structure is determined. With this analysis method, the aggregate structure of proteasome α7-subunit (PRSα) in an aqueous solution was investigated. Three structural models, a simple monomer and two types of dimers, were supposed as the aggregated structure of PRSα. The analysis showed that the best compromised structure was the dimer, which was consistent with electron microscopy observation.

Original languageEnglish
Pages (from-to)272-274
Number of pages3
JournalNuclear Instruments and Methods in Physics Research, Section A: Accelerators, Spectrometers, Detectors and Associated Equipment
Issue number1
Publication statusPublished - Feb 21 2009
Externally publishedYes


  • Complex protein
  • Large structure analysis
  • Proteasome
  • SANS
  • Solution scattering

ASJC Scopus subject areas

  • Nuclear and High Energy Physics
  • Instrumentation


Dive into the research topics of 'SANS simulation of aggregated protein in aqueous solution'. Together they form a unique fingerprint.

Cite this