UTOPIA-NMR: unified time-optimized interleaved acquisition NMR
Related funding:
Marie Sklodowska-Curie Individual Fellowship - EGFR-Activ (Grant agreement ID: 660258)
Schematic representation of the UTOPIA-NMR setup
Pulse sequence scheme for the unified acquisition of a 1H,15N-NOESY-TROSY (black) and a 13C,13C-FLOPSY (red)
Pulse sequence scheme for the unified acquisition of a 1H,15N-HNCA (black) and a 13C,15N-CON (red)
Schematic representation of the UTOPIA-NMR setup
A growing number of nuclear magnetic resonance (NMR) spectroscopic studies are impaired by the limited information content provided by the standard set of experiments conventionally recorded.
This is particularly true for studies of challenging biological systems including large, unstructured, membrane-embedded and/or paramagnetic proteins. Here we introduce the concept of unified time-optimized interleaved acquisition NMR (UTOPIA-NMR) for the unified acquisition of standard high-gamma (e.g. 1H) and low-gamma (e.g. 13C) detected experiments using a single receiver.
Our aim is to activate the high level of polarization and information content distributed on low-gamma nuclei without disturbing conventional magnetization transfer pathways. We show that using UTOPIA-NMR we are able to recover nearly all of the normally non-used magnetization without disturbing the standard experiments. In other words, additional spectra, that can significantly increase the NMR insights, are obtained for free.
|"...using UTOPIA-NMR we are able to recover nearly all of the normally non-used magnetization without disturbing the standard experiments.
This unified time-optimized interleaved acquisition offers a remarkable potential and flexibility for a multitude of applications. We anticipate that four areas of research will particularly benefit from the UTOPIA setup:
1. NMR analytics/screening of (small) compounds. Here the acquisition of 1D or 2D spectra of high-g (e.g. 1H, 19F) and low-g (e.g. 13C, 15N, 31P) nuclei can be carried out simultaneously, significantly reducing the total measurement time and increasing throughput.
2. The investigation of small soluble proteins at higher concentrations. Here excess in sensitivity can be split into additional experiments (using shared evolution periods).
3. The characterization of natively unfolded and/or paramagnetic proteins, which often focuses on the acquisition of a set of low-g-detected experiments. If low-g-detected experiments are the priority, UTOPIA-NMR can offer 1H-detected experiments for free.
4. . The investigation of perdeuterated biological systems including membrane proteins or large complexes.