both authors contributed equally to this work.
Cover Picture: Surface-Attached Polyhistidine-Tag Proteins Characterized by FTIR Difference Spectroscopy (ChemPhysChem 11/2012)
Article first published online: 27 JUL 2012
Copyright © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Volume 13, Issue 11, page 2617, August 6, 2012
How to Cite
Pinkerneil, P., Güldenhaupt, J., Gerwert, K. and Kötting, C. (2012), Cover Picture: Surface-Attached Polyhistidine-Tag Proteins Characterized by FTIR Difference Spectroscopy (ChemPhysChem 11/2012). ChemPhysChem, 13: 2617. doi: 10.1002/cphc.201290051
- Issue published online: 27 JUL 2012
- Article first published online: 27 JUL 2012
- Cited By
- difference spectroscopy;
- ir spectroscopy;
- reaction mechanisms
ATR-FTIR spectroscopy monitors protein reactions and interactions of monolayers at the atomic level. On p. 2649 K. Gerwert, C. Kötting et al. describe a method to immobilize proteins by means of a polyhistidine-tag and nitrilotriacetic-acid-modified lipids. Because polyhistidine tags are often used for protein purification, modified proteins are easy to access. This makes the method a universal technique for many soluble proteins. The setup allows the investigation of the secondary structure, orientation, reaction mechanisms and protein–ligand or protein–protein interactions.