Looped-PROjected SpectroscopY (L-PROSY): A simple approach to enhance backbone/sidechain cross-peaks in 1H NMR

Novakovic, Mihajlo; Cousin, Samuel F.; Jaroszewicz, Michael J.; Rosenzweig, Rina; Frydman, Lucio

doi:10.1016/j.jmr.2018.07.010

Cited by 20 publications

(37 citation statements)

References 41 publications

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“…Hadamard MT was introduced here as an extension of projective-measurement experiments where, instead of a looped t 1 time-domain encoding 15 , selective irradiations are used to impart significant SNR/unit_time gains in homonuclear correlation experiments involving fast-exchanging protons. To achieve these gains, HMT exploits the flow of water polarization to reset the states of the targeted sites, which are then perturbed away from equilibrium via selective saturation or inversions.…”

Section: Discussionmentioning

confidence: 99%

“…Possible drawbacks of relying on such high-field MT processes concern potential sample heating effects, but these were not found to be a problem even when operating at 1 GHz. Specificity in these MT experiments could be compromised by spin-diffusion among the non-labile 1 Hs in the system; we investigated a similar possibility for the case of L-PROSY, where it was found that a 1:1 correlation with conventional NOESY cross-peak intensities was preserved even in the presence of a spin-diffusion sink pool 15 . This correspondence will persist over a wide range of solvent exchange rates and correlation times; it remains to be investigated whether the continuous-irradiation or the repeated inversion versions of HMT, might perform differently in terms of potential spin-diffusion effects.…”

Section: Discussionmentioning

confidence: 99%

“…We have recently introduced Looped PROjective SpectroscopY (L-PROSY) 15 , an approach that alleviates these problems by regarding these exchange processes as “resets” within the framework of Anti-Zeno Effects 16 – 18 . Instead of applying a single mixing period for homonuclear transfers that will then reach kinetically-compromised amplitudes, L-PROSY “freezes” these transfers after they begin to act with their (fastest) initial rate, resets the labile 1 H states to their initial conditions by exploiting their exchange with an unperturbed solvent polarization reservoir, and repeats this process multiple times 19 , 20 .…”

Section: Introductionmentioning

confidence: 99%

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Sensitivity enhancement of homonuclear multidimensional NMR correlations for labile sites in proteins, polysaccharides, and nucleic acids

et al. 2020

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Multidimensional TOCSY and NOESY are central experiments in chemical and biophysical NMR. Limited efficiencies are an intrinsic downside of these methods, particularly when targeting labile sites. This study demonstrates that the decoherence imparted on these protons through solvent exchanges can, when suitably manipulated, lead to dramatic sensitivity gains per unit time in the acquisition of these experiments. To achieve this, a priori selected frequencies are encoded according to Hadamard recipes, while concurrently subject to looped selective inversion or selective saturation procedures. Suitable processing then leads to protein, oligosaccharide and nucleic acid cross-peak enhancements of ≈200–1000% per scan, in measurements that are ≈10-fold faster than conventional counterparts. The extent of these gains will depend on the solvent exchange and relaxation rates of the targeted sites; these gains also benefit considerably from the spectral resolution provided by ultrahigh fields, as corroborated by NMR experiments at 600 MHz and 1 GHz. The mechanisms underlying these experiments’ enhanced efficiencies are analyzed on the basis of three-way polarization transfer interplays between the water, labile and non-labile protons, and the experimental results are rationalized using both analytical and numerical derivations. Limitations as well as further extensions of the proposed methods, are also discussed.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Sensitivity enhancement of homonuclear multidimensional NMR correlations for labile sites in proteins, polysaccharides, and nucleic acids

et al. 2020

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“…A removable injector allows use of smaller sample volumes and minimises the disturbance of the magnetic field homogeneity. While originally not intended for measuring kinetics, dissolution DNP (see below) also uses rapid mixing to inject polarised water into the NMR tube, allowing triggering kinetics by adding a folding cofactor simultaneously with the polarised water, as shown recently (Chen et al, 2013;Novakovic et al, 2020a).…”

Section: Rapid Mixingmentioning

confidence: 99%

Real-time nuclear magnetic resonance spectroscopy in the study of biomolecular kinetics and dynamics

et al. 2021

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Abstract. The review describes the application of nuclear magnetic resonance (NMR) spectroscopy to study kinetics of folding, refolding and aggregation of proteins, RNA and DNA. Time-resolved NMR experiments can be conducted in a reversible or an irreversible manner. In particular, irreversible folding experiments pose large requirements for (i) signal-to-noise due to the time limitations and (ii) synchronising of the refolding steps. Thus, this contribution discusses the application of methods for signal-to-noise increases, including dynamic nuclear polarisation, hyperpolarisation and photo-CIDNP for the study of time-resolved NMR studies. Further, methods are reviewed ranging from pressure and temperature jump, light induction to rapid mixing to induce rapidly non-equilibrium conditions required to initiate folding.

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“…speed up the recording and further increase the time resolution. These techniques include different SOFAST and BEST-HMQC techniques (Favier and Brutscher, 2011; with longitudinal relaxation optimization (Farjon et al, 2009), Hadamard frequency encoding or ultrafast approaches (Gal et al, 2007) or in case of NOESY experiments Looped-PROjected SpectroscopY (L-PROSY) (Novakovic et al, 2020a(Novakovic et al, , 2018. Furthermore, several of the pulse sequences can be combined with non-uniform sampling (NUS) (Gołowicz et al, 2020) to further reduce the final measurement time up to a few seconds.…”

Section: General Pulse Scheme For Rt-nmrmentioning

confidence: 99%

Real-time NMR spectroscopy in the study of biomolecular kinetics and dynamics

Pintér

Hohmann

Grün

et al. 2021

Preprint

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Abstract. The review describes the application of NMR spectroscopy to study kinetics of folding, refolding and aggregation of proteins, RNA and DNA. Time-resolved NMR experiments can be conducted in a reversible or an irreversible manner. In particular irreversible folding experiments pose large requirements on (i) the signal-to-noise due to the time limitations and (ii) on synchronizing the refolding steps. Thus, this contribution discusses the application of methods for signal-to-noise increases including dynamic nuclear polarization, hyperpolarization and photo-CIDNP for the study of time-resolved NMR studies. Further, methods are reviewed ranging from pressure- and temperature-jump, light induction and rapid mixing to induce rapidly non-equilibrium conditions required to initiate folding.

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Looped-PROjected SpectroscopY (L-PROSY): A simple approach to enhance backbone/sidechain cross-peaks in 1H NMR

Cited by 20 publications

References 41 publications

Sensitivity enhancement of homonuclear multidimensional NMR correlations for labile sites in proteins, polysaccharides, and nucleic acids

Sensitivity enhancement of homonuclear multidimensional NMR correlations for labile sites in proteins, polysaccharides, and nucleic acids

Real-time nuclear magnetic resonance spectroscopy in the study of biomolecular kinetics and dynamics

Real-time NMR spectroscopy in the study of biomolecular kinetics and dynamics

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