Abstract
Multidimensional NMR techniques for the investigation of interactions between biological macromolecules and solvent molecules are discussed. Examples for the use of these techniques for the study of the interactions between urea and the DNA-binding domain of the 434-repressor which lead to unfolding of the polypeptide are given. These investigations show, that at low temperatures interaction between urea and the hydrophobic side chains of the protein can be detected. However, at temperatures above 293 K no binding of urea molecules to the polypeptide chain can be observed. Moreover, titration experiments with salts and non-ionic compounds show, that chemicals which act as kosmotropes can refold the protein even in 7 M urea. All these results suggest, that water molecules play an active role in the unfolding process of proteins.
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