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Updated: Apr 25, 2026

Examining the Conformational Dynamics of Membrane Proteins in situ with Site-directed Fluorescence Labeling
Published on: May 29, 2011
LDAI-based chemical labeling of intact membrane proteins and its pulse-chase analysis under live cell conditions
Takayuki Miki1, Sho-hei Fujishima1, Kazuhiro Komatsu1
1Department of Synthetic Chemistry and Biological Chemistry, Graduate School of Engineering, Kyoto University, Katsura, Nishikyo-ku, Kyoto 615-8510, Japan.
Abstract:
The functions of membrane proteins are tightly controlled by the dynamics such as protein trafficking and degradation. We demonstrated that ligand-directed acyl imidazole (LDAI) chemistry is broadly applicable to selective chemical labeling of various types of membrane-bound proteins under live cell conditions without a need for any tag fragments. The LDAI chemistry enabled pulse-chase analysis of these proteins to determine the half-life, as well as their degradation pathways by the imaging, under almost natural cellular conditions.
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