The following NMR experiments are usually recorded for unlabeled proteins:

• 1D ¹H spectrum of the protein dissolved in a mixture of 90% H₂O/10% D₂O or 100% D₂O solutions using some solvent suppression scheme.
• A series of 1D ¹H spectrum at several temperatures to observe the broadening or the shifting of resonance signals due to exchange, dynamic or folding processes.
• Study of chemical exhange processes by adding small amounts of D₂O and observe its effect on the labile NH proto resonances.
• Spectral assignment using 2D ¹H NMR experiments on both H₂O and D₂O solutions:
• 2D ¹H-¹H COSY-DQF experiment to trace out intraresidue J connectivities. E.COSY experiments can be also used to obtain J(HH) coupling constants.
• 2D ¹H-¹H TOCSY experiment to identify specific residues.
• 2D ¹H-¹H NOESY experiment to detect sequential and long-range through-space interactions. Obtention of distance anf J(HN-HA) coupling constraints.
• Protein dynamics from homonuclear relaxation studies: T₁, T₂ and NOE data.
• 2D ¹H-X heteronuclear correlation experiments can be also performed at natural abundance under special conditions.