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上田 祐生
no journal, ,
Microscopic structures in liquid-liquid extraction, such as structuration between extractants in bulk organic phases and at interfaces, can influence macroscopic phenomena, such as the distribution behavior of solutes and phase separation of the organic phase. We correlated the macroscopic behavior of the extraction of Zr(IV) ions from HNO
solutions with microscopic structural information in order to understand at the molecular level the key factors contributing to the higher metal ion extraction performance in the fluorous phosphate in perfluorohexane as compared to the analogous organic phosphate (THP) in n-hexane. Extended X-ray absorption fine structure (EXAFS), neutron reflectometry (NR), and small-angle neutron scattering revealed the local coordination structure around the Zr(IV) ion, the accumulation of extractant molecules at the interface, and the structuration of extractant molecules in the bulk extraction phase, respectively. In this study, deuteration of THP was performed to ensure a difference in neutron scattering length density between extractant and diluent in the NR experiment. This presentation will mainly report on the relationship between microscopic structural information obtained from EXAFS, NR, and SANS and macroscopic extraction behavior, and discuss the factors that give rise to differences between fluorous and organic extraction systems.
小田 隆
no journal, ,
Deuteration of samples is an important for structural analysis of biological macromolecules (proteins, nucleic acids) using neutron crystallography and small-angle neutron scattering (SANS). In the neutron crystallography, the use of fully deuterated proteins allows structural analysis with crystals smaller size than hydrogen proteins. In SANS, scattering from specific subunits or specific regions in protein complexes can be selectively observed by adjusting the deuteration rate of proteins and the concentration of heavy water in the solvent. For example, while a 75% deuterated protein is matched out in a 100% deuterated water solvent, light hydrogen proteins are not matched out under this condition, making it possible to specifically observe the scattering of light hydrogen proteins. Since the preparation of deuterated proteins requires a great deal of labor, we are developing a deuteration laboratory in J-PARC MLF and providing support for the preparation of deuterated samples for neutron users. In this session, we will talk the current state of deuteration laboratories and our research.
柴崎 千枝; 阿久津 和宏*; 上田 実咲*; 高田 慎一; 安達 基泰*
no journal, ,
Amino acids play a crucial role in physiological functions such as metabolism and immunity. Deuterated amino acids, in which some hydrogen atoms (H) are replaced with deuterium (D), are used to elucidate enzyme reaction mechanisms and analyze protein structures. Additionally, because the C-D bond in deuterated compounds is stronger than the C-H bond, deuteration enhances chemical stability. Investigating the properties of deuterated polymers, which have not been thoroughly studied, could lead to the development of new materials. We believe that developing deuteration techniques for amino acids and oligopeptides using metal catalysts at high temperatures can result in the creation of novel functional molecules.