Development of Analysis Method for Reconbinant Biomacromolecular System utlizing Neutron Scattering

2017 Fiscal Year Final Research Report

• Project/Area Number: 15H02042
• Research Category: Grant-in-Aid for Scientific Research (A)
• Allocation Type: Single-year Grants
• Section: 一般
• Research Field: Quantum beam science
• Research Institution: Kyoto University
• Principal Investigator: Sugiyama Masaaki 京都大学, 複合原子力科学研究所, 教授 (10253395)
• Co-Investigator(Kenkyū-buntansha): 加藤 晃一 名古屋市立大学, 大学院薬学研究科, 教授 (20211849) ; 矢木 宏和 名古屋市立大学, 大学院薬学研究科, 講師 (70565423) ; 井上 倫太郎 京都大学, 原子炉実験所, 准教授 (80563840) ; 藤井 紀子 京都大学, 原子炉実験所, 教授 (90199290)
• Co-Investigator(Renkei-kenkyūsha): TAKATA SHIN-ICHI 独立行政法人日本原子力研究開発機構, J-PARCセンター, 研究員 (70435600)
• Project Period (FY): 2015-04-01 – 2018-03-31
• Keywords: 蛋白質重水素化 / クラウディング / 中性子小角散乱 / コントラスト同調 / クリスタリン

Outline of Final Research Achievements

Biomacromolucle is functionalized in a polydispersed and high density system, namely a crowding system. Therefore, this study has developed a method to observe and analyze a structure and dynamics of a biomacromolucle in the crowding system. For this purpose, αB-crystallin which is eye lens protein is taken as a sample. A method to prepare 75% deuterated αB-crystallin was established and then it was confirmed that this protein is scatteringly invisible in 100% D2O solution. Based on the result, using the mixture of high concentration of 75% deuterated αB-crystallin with low concentration of not-deuterated αB-crystallin, which is one of crowding systems, it has been succeeded to observe not-deuterated αB-crystallin selectively with small-angle neutron scattering.

Free Research Field

ナノ構造物理学