Tobias Weidner and collaborators publish in Angewandte Chemie

The article describes how diatoms use proteins to build their cell walls out of nanostructured glass.

2017.06.22 | Susan Hjort Skyum

Understanding the structure of proteins at surfaces is key in fields such as biomaterials research, biosensor design, membrane biophysics and drug design. A particularly important factor is the orientation of proteins when bound to a particular surface. The orientation of the active site of enzymes or protein sensors, the availability of binding pockets within membrane proteins – these are important design parameters for engineers developing new sensors, surfaces and drugs. Recently developed methods to probe protein orientation, including immunoessays and mass spectrometry, either lack structural resolution or require harsh experimental conditions. We here report a new method to track the absolute orientation of interfacial proteins using phase resolved sum frequency generation spectroscopy in combination with molecular dynamics simulations and theoretical spectra calculations. As a model system we have determine the orientation of a helical lysine-leucine peptide at the air-water interface. The data show that the absolute orientation of the helix can be reliably determined even for orientations almost parallel to the surface.
Determination of Absolute Orientation of Protein α-Helices at Interfaces using Phase Resolved SFG Spectroscopy. Available from: https://www.researchgate.net/publication/317555612_Determination_of_Absolute_Orientation_of_Protein_a-Helices_at_Interfaces_using_Phase_Resolved_SFG_Spectroscopy [accessed Jun 14, 2017].  

Department of Chemistry, Staff, Public / media