TROSY for NMR Studies of Large Biological Macromolecules

Although collection of high-quality data for structure determination of proteins with molecular masses up to approximately 100 kDa is now technically feasible, the complexity of the NMR spectra generally increases with the size of the molecule studied and the concomitant signal overlap may limit spectral analysis, tterefore, the preferred current use of relaxation-optimized NMR techniques is with large structures that yield relatively simple spectra compared with spectra of monomeric globular proteins of the same molecular size, such as homo-oligomeric proteins, individual small or medium-sized subunits in large molecular complexes, and membrane proteins in detergent micelles (Wüthrich 1998; Fernández and Wider 2003).

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