Selective methyl group protonation of perdeuterated proteins.

By M. Rosen, Kevin H. Gardner, R. Willis, W. Parris, Tony Pawson, Lewis E. Kay. 1996

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Major Histocompatibility Complex (MHC) Class I and MHC Class II Proteins: Conformational Plasticity in Antigen Presentation (2017, methodology): “org March 2017 | Volume 8 | Article 292 For both MHC classes, more sophisticated NMR experiments capitalizing on selective amino acid side-chain labeling protocols are probably required and methods relying on CEST or relaxation dispersion should be able to yield more direct information on the antici”
Automated protein fold determination using a minimal NMR constraint strategy (2003, background): “A subsequent improved strategy is to protonate selective methyl groups in otherwise perdeuterated protein samples (Metzler et al. 1996; Rosen et al. 1996; Goto et al. 1999; Goto and Kay 2000).”
De novo protein structure determination using sparse NMR data (2000, background): “Using less information, low-resolution global folds can be obtained for large proteins that can greatly simplify resonance and constraint assignments (Venters et al., 1995; Rosen et al., 1996; Gardner et al., 1997; Battiste and Wagner, 2000).”
Protein structure determination by combining sparse NMR data with evolutionary couplings (2015, unknown): “Sparse NMR data is collected using uniformly 13 C, 15 N-enriched and/or 2 H, 13 C, 15 N-enriched protein samples prepared with 1 H-13 C labeling of sidechain Leu, Val, and Ile( δ ) methyl groups 3,5,21 .”