Environmentally Relevant Interfaces (ERI)

In the ERI group we use a combination of biochemical, and biophysical assays as well as state-of-the-art physicochemical experiments to advance our understanding of protein functions and chemical processes at environmentally relevant interfaces. Advanced spectroscopic tools such as surface-specific vibrational sum frequency generation spectroscopy allow us to detect processes in real time and directly at the relevant interfaces. Currently we are particularly interesed in ice-binding biomolecules and hydrophobins, which are proteins that show remarkable interfacial properties.

Antifreeze Proteins

Antifreeze Proteins

Controlling ice crystal growth is a grand scientific challenge with major technological ramifications for settings as diverse as oil fields, cryobiology, airplines and frozen food products. Ice formation is further lethal to most organisms. Antarctic fish living at subzero temperatures have evolved an elegant macromolecular solution to cope with this problem. They produce antifreeze proteins that are able to bind to ice crystal surfaces and arrest their growth. Upon binding to ice, the AFPs have overcome the apparent difficult problem of distinguishing the solid phase of water from the liquid that is present in vast excess. We are interested in unraveling the mode of action of these extraordinary molecules and tackle the problem by employing advanced spectroscopic and microscopic techniques.
<span>Ice Nucleation Proteins</span>

Ice Nucleation Proteins

Freeze-tolerant organisms such as insects or bacteria have taken the opposite approach to ensure survival at low temperatures. They use of ice nucleation proteins to promote ice growth at high subzero temperatures. INPs can promote the growth of ice more effectively than any other known substance and have relevance for various disciplines. Using various approaches we aim to study thed working mechanism of ice nucleation proteins.


Hydrophobins are a group of highly surface active proteins that are produced by fungi and are known for their unique functions related to the interaction and control of interfaces. They largely reduce the surface tension of water, strongly adhere to surfaces and form protective surface coatings, all functions that play important roles in fungal physiology. While much progress has been made in the characterization of the macroscopic structure of hydrophobin films, little is known about the initial stages of film formation and the microscopic structure of these unique proteins at interfaces.
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