The unfolded state of NTL9 is compact in the absence of denaturant

A model of the unfolded state of the N-terminal domain of ribosomal protein L9 (NTL9) in the absence of denaturant was generated by substitution of an alanine for phenylalanine 5 located in the core of this protein. Studies showed that the physiologically relevant unfolded state of wild-type NTL9 was more compact than the CD spectrum of the variant F5A since the mutation should reduce the level of hydrophobic clustering in the unfolded state in the absence of denaturant.