Kottke, Lórenz-Fonfría, and Heberle (2017). The Grateful Infrared: Sequential Protein Structural Changes Resolved by IR Difference Spectroscopy. J Phys Chem B 121, 335-350.
News from Jan 24, 2017
In the January 19, 2017 issue of The Journal of Physical Chemistry B, SFB member Joachim Heberle (project A1 and B3) and his co-workers published a Feature Article on "The Grateful Infrared: Sequential Protein Structural Changes Resolved by IR Difference Spectroscopy" (1). The article is accessible via the website of The Journal of Physical Chemistry B, a weekly published journal of the American Chemical Society (ACS).
In short, the authors showcase results from time-resolved IR spectroscopy on channelrhodopsin (ChR), light-oxygen-voltage (LOV) domain protein, and cryptochrome (CRY).
ACS has chosen one of the article's figures as the Journal Cover of the January 19, 2017 issue and explains it as follows: "Towards single molecule IR spectroscopy of proteins. The catalytic activity of proteins is linked to structural changes that the protein undergoes after activation. Infrared difference absorption spectroscopy is a potent methodology to resolve such structural changes. Kinetic infrared spectroscopy has been developed to trace the details of the reaction covering all time scales. Among other exciting novel developments, the recent progress in nanotechnology reaches a level of sensitivity that may allow for IR spectroscopy of single molecules. The cover illustrates a protein, here bacteriorhodopsin, that is tethered to gold nanoantenna serving as a plasmonic surface to enhance the vibrational response. The protein's vibrational spectrum will be probed in the optical near-field by IR radiation scattered at the tip of an atomic force microscope. Thereby, single molecule experiments may be conducted with the structural sensitivity of IR spectroscopy."(2)