Surface-attached polyhistidine-tag proteins characterized by FTIR difference spectroscopy.
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.
Lehrstuhl für Biophysik, Ruhr-Universität Bochum, 44780 Bochum, Germany.
Philipp
P
Pinkerneil
Jörn
J
Güldenhaupt
Klaus
K
Gerwert
Carsten
C
Kötting
D005857:Germanium / Q000737:chemistry; D006639:Histidine / Q000737:chemistry*; D055767:Immobilized Proteins / Q000737:chemistry; D008051:Lipid Bilayers / Q000737:chemistry; D008055:Lipids / Q000737:chemistry; D009571:Nitrilotriacetic Acid / Q000737:chemistry; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D017550:Spectroscopy, Fourier Transform Infrared; D013499:Surface Properties
D055767:Immobilized Proteins; D008051:Lipid Bilayers; D008055:Lipids; D011506:Proteins; D005857:Germanium; C033223:polyhistidine; D006639:Histidine; D009571:Nitrilotriacetic Acid