Steffen Graether
Professor
College of Biological Science
Department of Molecular and Cellular Biology
Guelph, Ontario
graether@uoguelph.ca
Office:
(519) 824-4120 ext. 56457
Expert In
Bio/Research
Dr. Graether's enthusiasm for studying antifreeze proteins has continued as an independent investigator. These intriguing proteins are found in a number of cold-environment organisms such as fish, insects, plants and bacteria. Though the freezing point is thought to be depressed through the “Kelv...
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Bio/Research
Dr. Graether's enthusiasm for studying antifreeze proteins has continued as an independent investigator. These intriguing proteins are found in a number of cold-environment organisms such as fish, insects, plants and bacteria. Though the freezing point is thought to be depressed through the “Kelvin Effect”, it is still unclear after many years of study how the protein binds to the ice surface. Graether's research group is interested in understanding how antifreeze protein binds to its ligand. They are studying the protein both in solution and in ice using NMR, and will test their models by measuring antifreeze activity of mutated and modified proteins.
A second project of Graether's involves the study of another stress-response protein known as dehydrin. These proteins are expressed in plants during times of desiccative stress, and are thought to bind water, protect the cellular membrane from drying and prevent proteins from denaturing. Dehydrins are predicted to be “intrinsically disordered proteins” (IDPs), meaning that they do not have a defined structure as we understand it. Graether and his research group are using NMR to characterize the flexibility of dehydrins and understand how they function.
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A second project of Graether's involves the study of another stress-response protein known as dehydrin. These proteins are expressed in plants during times of desiccative stress, and are thought to bind water, protect the cellular membrane from drying and prevent proteins from denaturing. Dehydrins are predicted to be “intrinsically disordered proteins” (IDPs), meaning that they do not have a defined structure as we understand it. Graether and his research group are using NMR to characterize the flexibility of dehydrins and understand how they function.
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