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Surface‐Attached Polyhistidine‐Tag Proteins Characterized by FTIR Difference Spectroscopy
Author(s) -
Pinkerneil Philipp,
Güldenhaupt Jörn,
Gerwert Klaus,
Kötting Carsten
Publication year - 2012
Publication title -
chemphyschem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.016
H-Index - 140
eISSN - 1439-7641
pISSN - 1439-4235
DOI - 10.1002/cphc.201200358
Subject(s) - nitrilotriacetic acid , attenuated total reflection , fourier transform infrared spectroscopy , chemistry , spectroscopy , infrared spectroscopy , lipid bilayer , analytical chemistry (journal) , chromatography , biochemistry , inorganic chemistry , chemical engineering , organic chemistry , membrane , physics , chelation , quantum mechanics , engineering
A universal label‐free method for the spectroscopic investigation of polyhistidine‐tagged proteins is presented. A solid supported lipid bilayer (SSLB, picture) containing nitrilotriacetic‐acid‐modified lipids is attached on top of a germanium attenuated total reflection crystal by hydrophilic interactions. Any His tag‐modified protein can be immobilized and investigated by FTIR spectroscopy.