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

NMR has unique potential for detailed structural characterization of d enatured states of proteins, provided that workable spectral resolutio n and sequence-specific assignments can be obtained in spite of the la ck of conformation-dependent dispersion of the H-1 chemical shifts. St ructures can be determined in the presence of dynamic conformational p olymorphism. This has recently been achieved for urea-unfolded bacteri ophage 434 repressor, and NMR assignments were determined for urea-unf olded FK 506-binding protein.