Symposium Sessions
Day 1, June 10（Wed.） 15:02-15:20 Room C (4F 413)
- 1C-S1-1502（1P-02）
Enhancing the Sensitivity of Kinase Accessibility-Based Structural Proteomics
(1Kyoto Univ., 2NCVC)
oAsato Maeda1, Kosuke Ogata1, Naoyuki Sugiyama1,2, Yasushi Ishihama1
MS-based protein structural analysis (protein footprinting) is increasingly being utilized to obtain a system-wide landscape of protein higher-order structural dynamics. Recently, we developed a protein footprinting method, termed phospho-labeler, which utilizes kinase accessibility as structural readout. In this study, we aimed to enhance the detectability of protein higher-order structural changes by exploring a broader range of kinase reaction conditions. By varying enzyme concentrations, we successfully increased the number of sites for which increased kinase accessibility was detectable upon disruption of substrate higher-order structure, compared with a single reaction condition. This result demonstrates that integrating multiple kinase reaction conditions enables highly sensitive profiling of protein higher-order structural changes.