Abstract
The synthesis of fluorescent unnatural amino-acid Anap was optimized and the Anap was incorporated into four sites in an acid-pocket or a transmembrane region of human acid-sensing ion channel-1a (hASIC1a). Combinational Anap fluorescence spectra and patch-clamp electrophysiology data illustrated site-specific conformational responses upon toxin mambalgin-1 binding. This combinational approach can be used to analyse conformational properties of many different eukaryotic proteins in their functional states, in a site-specific manner in live mammalian cells.
Original language | English (US) |
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Pages (from-to) | 8153-8156 |
Number of pages | 4 |
Journal | Chemical Communications |
Volume | 51 |
Issue number | 38 |
DOIs | |
State | Published - May 11 2015 |
Externally published | Yes |
ASJC Scopus subject areas
- General Chemistry
- Catalysis
- Ceramics and Composites
- Electronic, Optical and Magnetic Materials
- Surfaces, Coatings and Films
- Materials Chemistry
- Metals and Alloys
- General Medicine