Combining methods for speeding up multi-dimensional acquisition. Sparse sampling and fast pulsing methods for unfolded proteins.
Resonance assignment of intrinsically disordered proteins is made difficult by the extensive spectral overlaps. High-resolution 3D and 4D spectra are thus essential for this purpose. We have adapted the series of 3D BEST-experiments proposed by Lescop et al. [E. Lescop, P. Schanda, B. Brutscher, A set of BEST triple-resonance experiments for time-optimized protein resonance assignment, J. Magn. Reson. 187 (2007) 163-169] to the case of unfolded proteins. Longer acquisitions in the indirect dimensions are obtained by implementing semi-constant time evolution and sparse sampling. Using maximum entropy reconstruction for the indirect dimensions, the artifact intensity due to sparse sampling can be reduced to a level similar to the other sources of noise. The reduction of the sampled increments and the shorter duration of individual transients makes it possible to record a 4D experiment with reasonable resolution in less than 60 h.
Marion
Dominique
D
Laboratoire de RMN, Institut de Biologie Structurale Jean-Pierre Ebel, UMR5075 CNRS-CEA-UJF, 41, Rue Jules Horowitz, 38027 Grenoble Cedex, France. Dominique.Marion@ibs.fr
D048868:Adaptor Proteins, Signal Transducing / Q000737:chemistry; D000465:Algorithms; D016477:Artifacts; D019277:Entropy; D006515:Hepatitis B virus / Q000737:chemistry; D007090:Image Interpretation, Computer-Assisted / Q000295:instrumentation*; D009419:Nerve Tissue Proteins / Q000737:chemistry*; D017510:Protein Folding
D048868:Adaptor Proteins, Signal Transducing; C110719:LAMTOR5 protein, human; D009419:Nerve Tissue Proteins