2009年2月
SANS simulation of aggregated protein in aqueous solution
NUCLEAR INSTRUMENTS & METHODS IN PHYSICS RESEARCH SECTION A-ACCELERATORS SPECTROMETERS DETECTORS AND ASSOCIATED EQUIPMENT
- 巻
- 600
- 号
- 1
- 開始ページ
- 272
- 終了ページ
- 274
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1016/j.nima.2008.11.121
- 出版者・発行元
- ELSEVIER SCIENCE BV
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 alpha 7-subunit (PRS alpha) in an aqueous solution was investigated. Three structural models. a simple monomer and two types of dinners, were supposed as the aggregated structure of PRSa. The analysis showed that the best compromised structure was the dinner, which was consistent with electron microscopy observation. (C) 2008 Elsevier B.V. All rights reserved.
- リンク情報
- ID情報
-
- DOI : 10.1016/j.nima.2008.11.121
- ISSN : 0168-9002
- Web of Science ID : WOS:000264033800084