NMR is one of the few experimental methods that can provide detailed inside into the structure and dynamics of unfolded and partly folded states of proteins ( 96ENC3811 , 98ACR773 and 04CR3607 and 05METH299 ).

Protein folding can be studied from NMR by recording a series of 1D ¹H spectrum at several temperatures to observe the broadening or the shifting of resonance signals. In addition, correlation between the unfolded and the folded states can be performed using 1D or 2D NMR experiments that involves magnetization or saturation transfer as, for instance, the EXSY experiment.

Other NMR approaches to study protein folding:

• From amide hydrogen exchange ( 99JB65-15 )
• From diffusion coefficients ( 97JB199 , 00JACS5887 , 00BIO7910 )
• Amide proton temperature coefficients
• From dipolar couplings ( 99JB223 and 00JMB447 )
• Using Chemically induced dynamic nuclear polarization (CIDNP) ( 93PROG345 , 98ACR773 , 98NAT504 , 99JACS6505 , 00JB235 )
• From dynamic 1H NMR line shape analysis ( 96JMB311-263 , 98JMB1661-284 , and 99JMB763-293 )
• From relaxation data ( 01JMG3 ): T_1ro ¹⁵N measurements ( 00JACS5387 ) and ¹³C relaxation measurements ( 00JACS11610 ). Also for study and determine partially folded states ( 01JB3-19 )
• Calculation method (ASDEM) for rapid identification of ordered and disordered domains ( 96JACS8725 )
• Disordered states
• Use of secondary chemical shifts and cross-hydrogen ^3hbJ_NCO scalar coupling constants ( 01JB221-21 )

Examples of protein folding:

• Ribonuclease A or RNase A ( 88BIO2471 )
• Cytochrome c ( 88NAT700 ).
• Barnase ( 92JMB771 ).
• Apomyoglobin ( 90SCI1544 ).
• alpha-Lactalbumin ( 89BIO7 ).
• Lysozyme ( 91NAT633 , 92NAT302 , 92BIO4749 ).
• Staphylococcal nuclease A ( 86NAT192 , 89BIO362 ).
• Ubiquitin ( 92PNSA2017 ).
• Bovine pancreatic trypsin inhibitor (BPTI) ( 91SCI1386 ).