Abstract
NMR-based structural biology of proteins can be pursued efficiently in supercooled water at temperatures well below the freezing point of water. This enables one to study protein structure, dynamics, hydration and cold denaturation in an unperturbed aqueous solution at very low temperatures. Furthermore, such studies enable one to accurately measure thermodynamic parameters associated with protein cold denaturation. Presently available approaches to acquire NMR data for supercooled aqueous protein solutions are surveyed, new insights obtained from such studies are summarized, and future perspectives are discussed.
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