An overview of current methods employed for characterizing larger (>25 kDa) proteins by NMR is presented. These techniques include: the attenuation of T-2 relaxation effects by offsetting dipole-dipole and chemical shift anisotropy relaxation mechanisms (TROSY); the extraction of residual dipolar couplings from partially oriented molecules; the elimination of relaxation pathways by incorporating deuterium nuclei into protein samples; the easing of resonance overlap by isotopically labeling only specific protein segments; and the decrease of rotational correlation times by dissolving proteins in low viscosity solvents. (C) 2002 Elsevier Science B.V. All rights reserved.
Current approaches for the study of large proteins by NMR
Venters, RA., Thompson, R., & Cavanagh, J. (2002). Current approaches for the study of large proteins by NMR. Journal of Molecular Structure, 602, 275-292. [PII S0022-2860(01)00690-1].