Surface‐Attached Polyhistidine‐Tag Proteins Characterized by FTIR Difference Spectroscopy
Open Access
- 15 June 2012
- journal article
- research article
- Published by Wiley in Chemphyschem
- Vol. 13 (11) , 2649-2653
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.Keywords
This publication has 27 references indexed in Scilit:
- In Situ FTIR ATR Spectroscopic Study of the Interaction of Immobilized Human Serum Albumin with Cholate in Aqueous EnvironmentThe Journal of Physical Chemistry C, 2010
- Thinner, Smaller, Faster: IR Techniques To Probe the Functionality of Biological and Biomimetic SystemsAngewandte Chemie International Edition, 2010
- Dünner, kleiner, schneller - wie die IR-Spektroskopie zur Aufklärung des Funktionsmechanismus biologischer und biomimetischer Systeme beiträgtAngewandte Chemie, 2010
- The GAP arginine finger movement into the catalytic site of Ras increases the activation entropyProceedings of the National Academy of Sciences, 2008
- Functional waters in intraprotein proton transfer monitored by FTIR difference spectroscopyNature, 2005
- Proteins in Action Monitored by Time‐Resolved FTIR SpectroscopyChemphyschem, 2005
- Photoremovable Protecting Groups Used for the Caging of Biomolecules2005
- Structure of the I1 early intermediate of photoactive yellow protein by FTIR spectroscopyNature Structural & Molecular Biology, 2001
- Molecular Reaction Mechanisms of Proteins Monitored by Time-Resolved FTIR-SpectroscopyBiological Chemistry, 1999
- Reaction-induced infrared difference spectroscopy for the study of protein function and reaction mechanismsTrends in Biochemical Sciences, 1993