Type 1 AFP ice models
Other People/Labs working on AFP
Return to Lab home
Our laboratory applies nuclear magnetic resonance spectroscopy (NMR), other biophysical and computational methods towards the study of proteins structure, folding, dynamics and function. One focus of our investigations are antifreeze proteins from various fish species. These proteins bind to and inhibit the growth of ice nuclei of their solution or the fish serum, and thus keep it from freezing in an undercooled, metastable state. This facilitates the survival of fish in polar waters, where the sea water temperature is 1 °C below the freezing point of the fish blood. This non-colligative or kinetic freezing point depression is a fascinating, unique activity for proteins. It is not only of fundamental interest but also of commercial interest due to several possible applications in agriculture and medical areas.
Antifreeze proteins have been identified in many organisms exposed to freezing stress. They are found in bacteria, plants, insects, and fish, but only the latter twoare biochemically characterized. Four types of fish antifreeze proteins are known to date, antifreeze glycoproteins and Type 1, 2 and 3 antifreeze proteins. They are biochemically extremely diverged which includes their primary, secondary and tertiary structure. Despite their fundamental differences, they converged functionally and have been shown to similarly bind to ice crystals.
Type 1 AFP ice models
Other People/Labs working on AFP
Return to Lab home