Program

Poster Presentations

Day 2, May 16（Wed.）　　Poster

2P-20　　PDF

Characterization of deuterated α-crystalline using bench-top MALDI-TOFMS.

(¹Shimadzu, ²Kyoto Univ.)
^oYuzo Yamazaki¹, Ken Morishima², Nobuhiro Sato², Rintaro Inoue², Masaaki Sugiyama²

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.