Global folds of highly deuterated, methyl-protonated proteins by multidimensional NMR.

By Kevin H. Gardner, M. Rosen, Lewis E. Kay. 1997

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Citations in the corpus

Critical Assessment of Methods of Protein Structure Prediction (CASP) – Progress and New directions in Round XI (2016, methodology): “29,33–36 The ASDP program37–39 was then used to generate an initial set of both unique and ambiguous distance atom pair restraints from these NOESY peak lists.”
Automated protein fold determination using a minimal NMR constraint strategy (2003, methodology): “Based on the above technical advances in the field of protein NMR, and motivated by recent successes of obtaining correct folds by manual analysis of sparse NMR data (Gardner et al. 1997; Medek et al. 2000), we are developing largely automated approaches for determining medium-accuracy protein struc”
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 .”
De novo protein structure determination using sparse NMR data (2000, background): “This set was stochastically paired to be consistent with the empirical distance dependent frequency with which NOEs of neighboring atoms areunobserved due to solvent exchange, resonance degeneracy, or rapid relaxation processes (Doreleijers et al., 1999).”
Rapid and accurate calculation of protein 1H, 13C and 15N chemical shifts (2003, background): “Currently SHIFTX does not include deuterium isotope effects in predicting 13C and 15N shifts (Bjorndahl et al., 2001; Gardner et al., 1997).”