ポスター発表
- 第2日 5月16日(水) ポスター会場
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2P-20 PDF
卓上型MALDI-TOFMSによる重水素化α-crystallineのキャラクタリゼーション
Deuteration of protein is a one of the important technique in structural biology by using NMR or neutron scattering method. Incorporation of deuterated subunit protein into the hydrogenated one brings a new aspect of molecular dynamics in formation of multimer. As recent techniques for the deuteration have been more precise and more cost-effective, a quick and facile method to check deuterated proteins has been anticipated. In this report, we applied newly developed bench-top MALDI-TOFMS to analysis of deuterated αB-crystalline to study substitution of hydrogen to deuterium in three different ways, molecular weight analysis, in-source decay, and tryptic peptide analysis. Furthermore, we will report multimer formation of the protein by using high mass detector and cross-linking chemistry.