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
N1 - Funding Information:
The authors thank Dr. Keiji Tanaka of Tokyo Metropolitan Institute of Medical Science for providing us with the expression system of human proteasome α7 subunit. The SANS experiment was performed at SAND under the contract no 4787. The authors greatly appreciate to Dr. Thiyagarajan of Argonne National Laboratory for his help with the SANS experiment at SAND. The authors also would like to thank Prof. Chatake of Kyoto University for his kind help with operation of CNS program. This work is partially supported by Creative Scientific Research (no.16GS0417), Priority Areas (no.18076003), Grant-in-Aid for Scientific Research, Ministry of Education, Culture, Sports, Science and Technology. The authors are also supported by Grant-in-Aid for Scientific Research of the Ministry of Education, Science and Culture, Japan (no.19540427, no.19570103 and no.18310148). Y.M. and K.K. are supported by Target Protein Project from the Ministry of Education, Culture, Sports, Science and Technology of Japan.
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
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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 -