• Name: Konrad Meister, Ph.D.
  • Institution: Boise State University
  • Department: Chemistry
  • Phone: 907-419-5320
  • Email: konradmeister@boisestate.edu

Summary: My overreaching research aim is to obtain an understanding of the molecular strategies of cold-adapted organisms in response to environmental stress. This is a central question for scientific goals as diverse as the production of antifreeze proteins in cold-stressed plants, insects, fish or microbes; or the analysis of biological residues as potential sources of atmospheric ice nuclei. More specifically, I am interested in identifying novel antifreeze and ice nucleating proteins from different biological sources, and to investigate their structure, working mechanisms and possible applications. To achieve these goals I am using a combination of biochemical, and biophysical assays as well as state-of-the-art physicochemical (spectroscopic) experiments.

Minimum classes: No minimum classes required if you are motivated.  General Chemistry or Biochemistry would be helpful though

Projects: In my 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. Currently we are particularly interested in ice-binding biomolecules and hydrophobins, which are both proteins with remarkable interfacial properties.

(I)Antifreeze Proteins

Controlling ice crystal growth is a grand scientific challenge with major technological ramifications for settings as diverse as oil fields, cryobiology, airlines 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.

(II) Ice Nucleating Proteins

Freeze-tolerant organisms such as insects or bacteria have taken the opposite approach to ensure survival at low temperatures. They use 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.

(III) Hydrophobins

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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