NMR ASSIGNMENTS AS A BASIS FOR STRUCTURAL CHARACTERIZATION OF DENATURED STATES OF GLOBULAR-PROTEINS

NMR has unique potential for detailed structural characterization of denatured states of proteins, provided that workable spectral resolution and sequence-specific assignments can be obtained in spite of the lack of conformation-dependent dispersion of the H-1 chemical shifts. Structures can be determined in the presence of dynamic conformational polymorphism. This has recently been achieved for urea-unfolded bacteriophage 434 repressor, and NMR assignments were determined for urea-unfolded FK 506-binding protein.