Abstract
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 language | English |
|---|---|
| Pages (from-to) | 272-274 |
| Number of pages | 3 |
| Journal | Nuclear Instruments and Methods in Physics Research, Section A: Accelerators, Spectrometers, Detectors and Associated Equipment |
| Volume | 600 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - Feb 21 2009 |
| Externally published | Yes |
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Keywords
- Complex protein
- Large structure analysis
- Proteasome
- SANS
- Solution scattering
ASJC Scopus subject areas
- Instrumentation
- Nuclear and High Energy Physics
Cite this
SANS simulation of aggregated protein in aqueous solution. / Sugiyama, Masaaki; Hamada, Kei; Kato, Koichi; Kurimoto, Eiji; Okamoto, Kenta; Morimoto, Yukio; Ikeda, Susumu; Naito, Sachio; Furusaka, Michihiko; Itoh, Keiji; Mori, Kazuhiro; Fukunaga, Toshiharu.
In: Nuclear Instruments and Methods in Physics Research, Section A: Accelerators, Spectrometers, Detectors and Associated Equipment, Vol. 600, No. 1, 21.02.2009, p. 272-274.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - SANS simulation of aggregated protein in aqueous solution
AU - Sugiyama, Masaaki
AU - Hamada, Kei
AU - Kato, Koichi
AU - Kurimoto, Eiji
AU - Okamoto, Kenta
AU - Morimoto, Yukio
AU - Ikeda, Susumu
AU - Naito, Sachio
AU - Furusaka, Michihiko
AU - Itoh, Keiji
AU - Mori, Kazuhiro
AU - Fukunaga, Toshiharu
PY - 2009/2/21
Y1 - 2009/2/21
N2 - 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.
AB - 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.
KW - Complex protein
KW - Large structure analysis
KW - Proteasome
KW - SANS
KW - Solution scattering
UR - http://www.scopus.com/inward/record.url?scp=59649114002&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=59649114002&partnerID=8YFLogxK
U2 - 10.1016/j.nima.2008.11.121
DO - 10.1016/j.nima.2008.11.121
M3 - Article
AN - SCOPUS:59649114002
VL - 600
SP - 272
EP - 274
JO - Nuclear Instruments and Methods in Physics Research, Section A: Accelerators, Spectrometers, Detectors and Associated Equipment
JF - Nuclear Instruments and Methods in Physics Research, Section A: Accelerators, Spectrometers, Detectors and Associated Equipment
SN - 0168-9002
IS - 1
ER -