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Surface-attached polyhistidine-tag proteins characterized by FTIR difference spectroscopy.

ABSTRACT: 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.

SUBMITTER: Pinkerneil P 

PROVIDER: S-EPMC3531609 | biostudies-literature | 2012 Aug

REPOSITORIES: biostudies-literature

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Surface-attached polyhistidine-tag proteins characterized by FTIR difference spectroscopy.

Pinkerneil Philipp P   Güldenhaupt Jörn J   Gerwert Klaus K   Kötting Carsten C  

Chemphyschem : a European journal of chemical physics and physical chemistry 20120615 11

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. ...[more]

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