NMR with Multiple Receivers

Agilent Technologies, NMR and MRI Systems, Yarnton, Oxford, OX5 1QU, UK, .
Topics in current chemistry (Impact Factor: 4.46). 08/2011; 335. DOI: 10.1007/128_2011_226
Source: PubMed


Parallel acquisition NMR spectroscopy (PANSY) is used to detect simultaneously signals from up to four nuclear species, such as H-1, H-2, C-13, N-15, F-19 and P-31. The conventional COSY, TOCSY, HSQC, HMQC and HMBC pulse sequences have been adapted for such applications. Routine availability of NMR systems that incorporate multiple receivers has led to development of new types of NMR experiments. One such scheme named PANACEA allows unambiguous structure determination of small organic molecules from a single measurement and includes an internal field/frequency correction routine. It does not require the conventional NMR lock system and can be recorded in pure liquids. Furthermore, long-range spin-spin couplings can be extracted from the PANACEA spectra and used for three-dimensional structure refinement. In bio-molecular NMR, multi-receiver NMR systems are used for simultaneous recording of H-1 and C-13 detected multi-dimensional spectra. For instance, the 2D (HA)CACO and 3D (HA)CA(CO)NNH experiments can be recorded simultaneously in proteins of moderate size (up to 30 kDa). The multi-receiver experiments can also be used in combination with the fast acquisition schemes such as Hadamard spectroscopy, computer optimized aliasing and projection-reconstruction techniques. In general, experiments that utilize multiple receivers provide significantly more information from a single NMR measurement as compared to the conventional single receiver techniques.

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    ABSTRACT: We describe here, adaptation of the HNN pulse sequence for multiple nuclei detection using two independent receivers by utilizing the detectable (13)C(α) transverse magnetization which was otherwise dephased out in the conventional HNN experiment. It enables acquisition of 2D (13)C(α)-(15)N sequential correlations along with the standard 3D (15)N-(15)N-(1)H correlations, which provides directionality to sequential walk in HNN, on one hand, and enhances the speed of backbone assignment, on the other. We foresee that the implementation of dual direct detection opens up new avenues for a wide variety of modifications that would further enhance the value and applications of the experiment, and enable derivation of hitherto impossible information.
    No preview · Article · Dec 2011 · Journal of Biomolecular NMR
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    ABSTRACT: We introduce the use of multiple receivers applied in parallel for simultaneously recording multi-dimensional data sets of proteins in a single experiment. The utility of the approach is established through the introduction of the 2D (15)N,(1)H(N)||(13)CO HSQC experiment in which a pair of two-dimensional (15)N,(1)H(N) and (15)N,(13)CO spectra are recorded. The methodology is further extended to higher dimensionality via the 3D (1)H(N)||(13)CO HNCA in which a pair of data sets recording (13)C(α),(15)N,(1)H(N) and (13)C(α),(15)N,(13)CO chemical shifts are acquired. With the anticipated increases in probe sensitivity it is expected that multiple receiver experiments will become an important approach for efficient recording of NMR data.
    No preview · Article · Jul 2012 · Journal of Biomolecular NMR
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    ABSTRACT: We present here an NMR pulse sequence with 5 independent incrementable time delays within the frame of a 3-dimensional experiment, by incorporating polarization sharing and dual receiver concepts. This has been applied to directly record 3D-HA(CA)NH and 3D-HACACO spectra of proteins simultaneously using parallel detection of (1)H and (13)C nuclei. While both the experiments display intra-residue backbone correlations, the 3D-HA(CA)NH provides also sequential 'i - 1 → i' correlation along the (1)Hα dimension. Both the spectra contain special peak patterns at glycine locations which serve as check points during the sequential assignment process. The 3D-HACACO spectrum contains, in addition, information on prolines and side chains of residues having H-C-CO network (i.e., (1)Hβ, (13)Cβ and (13)COγ of Asp and Asn, and (1)Hγ, (13)Cγ and (13)COδ of Glu and Gln), which are generally absent in most conventional proton detected experiments.
    No preview · Article · May 2013 · Journal of Biomolecular NMR
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