Proteins employed in NMR studies can be deuterated at several levels:

Perdeuteration at nonexchangeable sites:

Facilitate the process of sequential backbone and side-chain assignments ( 93JACS4369 , 94JACS6464 , 94JACS11655 , 95JACS4187 ).

Reduce NOE spin diffusion in a general way ( 88BIO142 and 88JACS2320 ).

Observation of NOE contacts between exchangeable NH protons with high sensitivity.

Partial random deuteration at 50%-70% level:

Optimizes the sensitivity of experiments which are used for side-chain assignment purposes and to obtain NOE data ( 96JACS407 ).

Site specific protonation of an otherwhise highly deuterated proteins has been reported. This approach maintains the high efficiency of triple resonance methods while retaining suficient protons to establish useful long-range NOE contacts.

Protonated HA position ( 97JACS872 )

Protonated methyl groups ( 96JB351 , 97BIO1389 )

Selective protonation of the methyl groups of Ile, Leu and Val residues ( 96JACS6800 , 97JACS7599 , 98JACS11738 , 99JB369 )

Selective ¹³C of the methyl groups of Ile, Leu and Val residues and protonated Phe and Tyr ( 00JB229-18 ).

96JMB627 , 96JB360 , 98JACS4825

Selective deuteration of HA atoms ( 96STR1245 ).

Other approaches:

Specific protonation and ¹⁴N-labeling of the residues Phe, Tyr, Thr, Ile, and Val in a ²H,¹⁵N-labeled protein ( 99JB79 ).

Exclusive isotopic labeling in the backbone atoms ( 99JACS11871 ) in order to remove the interference of one-bond CA-CB coupling constants.

Optimized labeling of ¹³CHD₂ methyl isotopomers in perdeuterated proteins ( 01JB167-21 )

Use of 13CO-13CA-15N-2HA labeled proteins. The absence of CA-CB coupling allows to measure data from non contant-time pulse schemes ( 02JB21-22 )

Comparison of 13CH3, 13CH2D, 13CHD2 methyl labeling strategies ( 05JB25-33 )