Abstract
The set of tools offered to NMR spectroscopists has been greatly expanded in the last decades with the development of computer processing power. It has facilitated the use of non-Fourier transform reconstruction algorithms, leading to the ability to acquire data using non-uniform sampling. Its use in solid-state NMR, especially for biological systems, emerges as the next leap toward the analysis and structure prediction of large proteins. Here we applied various non-uniform sampling schemes to assess their performance towards a three-dimensional N−C−C correlation experiment aimed to assign chemical shifts in the coat protein of an intact filamentous bacteriophage fd virus. We show that using the sparse multidimensional iterative lineshape-enhanced (SMILE) reconstruction algorithm, biased sampling increases signal-to-noise without compromising linewidths and accuracy of chemical shift determination.
Original language | English |
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Pages (from-to) | 1027-1038 |
Number of pages | 12 |
Journal | Israel Journal of Chemistry |
Volume | 59 |
Issue number | 11-12 |
DOIs | |
State | Published - 1 Nov 2019 |
Keywords
- fd virus
- filamentous bacteriophages
- magic angle spinning
- non-uniform sampling
- solid-state NMR
All Science Journal Classification (ASJC) codes
- General Chemistry