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Measurement of scalar couplings between protons is a very challenging task because of complex multiplet patterns and severe overlapping of these multiplets in congested 1D spectra. Numerous 2D J‐resolved sequences now exist that utilize either the Zangger‐Sterk or PSYCHE or z‐filter elements along with selective refocusing and pure‐shift schemes to generate high‐resolution phase‐sensitive spectra with simple doublets in F1$$ {F}_1 $$ dimension. Herein, we present a 2D J‐resolved sequence that employs a simple element consisting of hard pulses and inter‐pulse delays to generate phase‐sensitive spectra. This simple element in combination with selective refocusing eliminates all the undesired components including the intense axial peaks, thus provides clean 2D J‐resolved spectra with signals of only two targeted protons with simple doublets in F1$$ {F}_1 $$ dimension and full multiplets of target protons in F2$$ {F}_2 $$ dimension. This high selectivity thus obviates the need for extra filtering elements and pure‐shift acquisition schemes that are integrated into existing sequences to facilitate coupling measurements in overcrowded signals. It is therefore anticipated that this sequence, with the ease of implementation and ability to extract coupling values from highly congested spectra, should turn out an important tool for structural and conformational analyses in chemical and biological studies. [ABSTRACT FROM AUTHOR]

Two-dimensional J-resolved (2D JRES) nuclear magnetic resonance (NMR) experiments provide a simple and user-friendly spectral representation, in which J couplings and chemical shifts are separated into two orthogonal frequency dimensions. The 2D JRES experiments have attracted wide attention in fundamental pulse sequence developments and practical applications, since they were first proposed 40 years ago. In this paper, we review the recent advances in the development of novel 2D JRES pulse sequences and 2D J-edited methods for accurate measurements of J coupling, mainly focusing on pure shift based 2D orthogonal-pattern and phase-sensitive 2D JRES spectroscopy and their applications in overcoming strong coupling effects and field inhomogeneities.

Magnetic resonance spectroscopy (MRS) is a powerful tool capable of investigating the metabolic status of several tissues in vivo. In particular, single-voxel-based 1 H spectroscopy provides invaluable biochemical information from a volume of interest (VOI) and has therefore been used in a variety of studies. Unfortunately, typical one-dimensional MRS data suffer from severe signal overlap and thus important metabolites are difficult to distinguish. One method that is used to disentangle overlapping resonances is the two-dimensional J-resolved spectroscopy (JPRESS) experiment. Due to the long acquisition duration of the JPRESS experiment, a limited number of points are acquired in the indirect dimension, leading to poor spectral resolution along this dimension. Poor spectral resolution is problematic because proper peak assignment may be hindered, which is why the zero-filling method is often used to improve resolution as a post-processing step. However, zero-filling leads to spectral artifacts, which may affect visualization and quantitation of spectra. A novel method utilizing a covariance transformation, called covariance J-resolved spectroscopy (CovJ), was developed in order to improve spectral resolution along the indirect dimension (F1 ). Comparison of simulated data demonstrates that peak structures remain qualitatively similar between JPRESS and the novel method along the diagonal region (F1 = 0 Hz), whereas differences arise in the cross-peak (F1 ≠0 Hz) regions. In addition, quantitative results of in vivo JPRESS data acquired on a 3T scanner show significant correlations (r2 >0.86, p

Purpose The echo time (TE) averaged spectrum is the one-dimensional (1D) cross-section of the J-resolved spectrum at J = 0. In multiecho TE-averaged spectroscopy, glutamate (Glu) is differentiated from glutamine (Gln) at 3 Tesla (T). This method, however, almost entirely suppresses Gln resonance lines around 2.35 ppm, leaving Gln undetermined. This study presents a novel method for quantifying both Glu and Gln using multi-echo spectral data. Methods A 1D cross-section of J-resolved spectroscopy at J = 7.5 Hz-referred to as J-modulated spectroscopy-was developed to simultaneously quantify Glu and Gln levels in the human brain. The transverse relaxation times (T2s) of metabolites were first determined using conventional TE-averaged spectroscopy with different starting echo time and then incorporated into the spectral model for fitting J-modulated data. Results Simulation and in vivo data showed that the resonance signals of Glu and Gln were clearly separated around 2.35 ppm in J-modulated spectroscopy. In the anterior cingulate cortex, both Glu and Gln levels were found to be significantly higher in gray matter than in white matter in healthy subjects ( P < 10−10 and < 10−5, respectively). Conclusion Gln resonances can be clearly separated from Glu and N-acetyl-aspartate around 2.35 ppm using J-modulated spectroscopy. This method can be used to quantitatively measure Glu and Gln simultaneously at 3T. Magn Reson Med 76:725-732, 2016. Published 2015. This article is a U.S. Government work and is in the public domain in the USA. [ABSTRACT FROM AUTHOR]

Nuclear magnetic resonance (NMR) spectroscopy provides a powerful tool for food analyses due to its high-throughput information related to component analyses and its non-invasive property without altering detected samples. Current liquid NMR approaches, however, are subject to the influence of field inhomogeneity in direct measurements of biological foods, generally resorting to techniques of tissue extractions or magic-angle spin to eliminate the inhomogeneity. Therefore, we propose an NMR approach based on intermolecular double-quantum coherences (iDQCs) and spatial encoding technique to fast recover high-resolution two-dimensional (2D) J-resolved spectra in inhomogeneous fields. Inheriting from the immunity to field inhomogeneity of iDQCs and the enhancement in acquisition efficiency of the spatial encoding technique, the proposed method can resist the field inhomogeneity in biological foods without superfluous pretreatments and time-consuming shimming procedures, and yield satisfactory 2D J-resolved information for analyses within minutes. Fish and its products, which are closely related to human daily life, capture extensive attentions with the rapid development of the aquaculture. At first, experiments on cod liver oils are implemented in a purposely deshimmed magnetic field to demonstrate the feasibility of the proposed approach. Then, caviars and an intact fish are tested to further show the applicability of the proposed approach for direct measurements on intact biological food samples. Herein, the proposed method may constitute an effective technique in analyzing fish and its products. [ABSTRACT FROM AUTHOR]

Abstract: The use of two-dimensional heteronuclear J-resolved (2D H-JRES) nuclear magnetic resonance (NMR) spectroscopy for fast and reliable measurement of isotopic patterns from 13C-enriched compounds resulting from carbon labeling experiments was evaluated. Its use with biological samples of increasing complexity showed that 2D H-JRES spectroscopy is suitable for high-throughput isotopic profiling of any kind of labeled samples. Moreover, the method enabled accurate quantification of 13C enrichments and, thus, can be used for metabolic flux analysis. The excellent trade-off between reduced experimental time and the number of measurable isotopic data makes 2D H-JRES NMR a promising approach for high-throughput flux analysis of samples of intermediate complexity. [Copyright &y& Elsevier]

Abstract: High-resolution 2D NMR spectra in inhomogeneous fields can be achieved by the use of intermolecular multiple-quantum coherences and shearing reconstruction of 3D data. However, the long acquisition time of 3D spectral data is generally unbearable for in vivo applications. To overcome this problem, two pulse sequences dubbed as iDH-COSY and iDH-JRES were proposed in this paper. Although 3D acquisition is still required for the new sequences, the high-resolution 2D spectra can be obtained with a relatively short scanning time utilizing the manipulation of indirect evolution period and sparse sampling. The intermolecular multiple-quantum coherence treatment combined with the raising and lowering operators was applied to derive analytical signal expressions for the new sequences. And the experimental observations agree with the theoretical predictions. Our results show that the new sequences possess bright perspective in the applications on in vivo localized NMR spectroscopy. [ABSTRACT FROM AUTHOR]

Abstract: Recent ultrafast techniques make it possible to obtain nD NMR spectra in a single scan. However, an important sensitivity decrease is observed when the excitation duration is increased, which is necessary to improve resolution. A detailed, theoretical and experimental study of sensitivity losses in ultrafast experiments is carried out on the example of J-resolved spectroscopy. The importance of molecular diffusion effects during both encoding and acquisition phases is shown by numerical simulations and experimental results. Other possible sources of signal-to-noise decrease are also considered, such as transverse relaxation, homonuclear J-couplings or chemical shift effects. [Copyright &y& Elsevier]

Abstract: Two dimensional (2D) homonuclear 1H J-resolved (JRES) nuclear magnetic resonance spectroscopy is increasingly used in metabolomics. This approach visualises metabolite chemical shifts and scalar couplings along different spectral dimensions, thereby increasing peak dispersion and facilitating spectral assignments and accurate quantification. Here, we optimise the processing of 2D JRES spectra by evaluating different window functions, a traditional sine-bell (SINE) and a combined sine-bell–exponential (SEM) function. Furthermore, we evaluate different projection methods for generating 1D projected spectra (pJRES). Spectra were recorded from three disparate types of biological samples and evaluated in terms of sensitivity, reproducibility and resolution. Overall, the SEM window function yielded considerably higher sensitivity and comparable spectral reproducibility and resolution compared to SINE, for both 1D pJRES and 2D JRES datasets. Furthermore, for pJRES spectra, the highest spectral quality was obtained using SEM combined with skyline projection. These improvements lend further support to utilising 2D J-resolved spectroscopy in metabolomics. [Copyright &y& Elsevier]

Abstract: Recent ultrafast techniques enable nD NMR spectra to be obtained in a single scan. However, resolution enhancement in the ultrafast domain leads to important sensitivity losses and lineshape distortions. In order to understand better resolution and spatial encoding aspects of continuous phase-encoding schemes, a theoretical and experimental comparison of different excitation patterns is carried out. Molecular diffusion appears to be the main cause of signal-to-noise ratio decrease, and a multi-echo excitation scheme is proposed to limit its effects when a good resolution is needed. Results obtained on 2D J-resolved spectra are presented. [Copyright &y& Elsevier]

Abstract: In this work a combination of complementary advanced solid-state nuclear magnetic resonance (NMR) strategies is employed to analyse the network organization in aluminophosphate glasses to an unprecedented level of detailed insight. The combined results from MAS, MQMAS and 31P-{27Al}-CP-heteronuclear correlation spectroscopy (HETCOR) NMR experiments allow for a detailed speciation of the different phosphate and aluminate species present in the glass. The interconnection of these local building units to an extended three-dimensional network is explored employing heteronuclear dipolar and scalar NMR approaches to quantify P–O–Al connectivity by 31P{27Al}-heteronuclear multiple quantum coherence (HMQC), -rotational echo adiabatic passage double resonance (REAPDOR) and -HETCOR NMR as well as 27Al{31P}-rotational echo double resonance (REDOR) NMR experiments, complemented by 31P-2D-J-RESolved MAS NMR experiments to probe P–O–P connectivity utilizing the through bond scalar J-coupling. The combination of the results from the various NMR approaches enables us to not only quantify the phosphate units present in the glass but also to identify their respective structural environments within the three-dimensional network on a medium length scale employing a modified Q notation, Q n m ,AlO x , where n denotes the number of connected tetrahedral phosphate, m gives the number of aluminate species connected to a central phosphate unit and x specifies the nature of the bonded aluminate species (i.e. 4, 5 or 6 coordinate aluminium). [Copyright &y& Elsevier]

Abstract: Recent ultrafast techniques enable 2D NMR spectra to be obtained in a single scan. A modification of the detection scheme involved in this technique is proposed, permitting the achievement of 2D 1H J-resolved spectra in 500ms. The detection gradient echoes are substituted by spin echoes to obtain spectra where the coupling constants are encoded along the direct ν 2 domain. The use of this new J-resolved detection block after continuous phase-encoding excitation schemes is discussed in terms of resolution and sensitivity. J-resolved spectra obtained on cinnamic acid and 3-ethyl bromopropionate are presented, revealing the expected 2D J-patterns with coupling constants as small as 2Hz. [Copyright &y& Elsevier]

The saturation transfer difference (STD) experiment is a rich source of information on topological aspects of ligand binding to a receptor. The epitope mapping is based on a magnetization transfer after signal saturation from the receptor to the ligand, where interproton distances permit this process. Signal overlap in the STD spectrum can cause difficulties to correctly assign and/or quantitate the measured enhancements. To address this issue we report here a modified version of the routine experiment and a processing scheme that provides a 1D-STD homodecoupled spectrum (i.e. an experiment in which all STD signals appear as singlets) with line widths similar to those in original STD spectrum. These refinements contribute to alleviate problems of signal overlap. The experiment is based on 2D-J-resolved spectroscopy, one of the fastest 2D experiments under conventional data sampling in the indirect dimension, and provides excellent sensitivity, a key factor for the difference experiments. [ABSTRACT FROM AUTHOR]

Abstract: A major problem in J-resolved spectroscopy and many other experiments is the appearance of “artefacts” due to strong coupling. The signals giving rise to these artefacts follow the same coherence transfer pathways as the required signals, making it impossible to suppress them using phase cycling or pulsed field gradients. We present new methods for suppressing these artefacts, applicable to any experiment containing a J-resolved pulse sequence element, as well as to constant-time experiments. [Copyright &y& Elsevier]

• Double spin-echo sequence is proposed for measuring homonuclear J-couplings. • Weak J-coupling constants less than intrinsic natural linewidths can be measured. • This method is capable of obtaining hydrogen-mediated 15N-15N J-couplings. The tautomeric structure and chemistry of the histidine imidazole ring play active roles in many structurally and functionally important proteins and polypeptides. While in NMR spectroscopy histidine chemical shifts (e.g. 15N, 13C, and 1H) have been commonly used to characterize the tautomeric structure, hydrogen bonding, and torsion angles, homonuclear 15N scalar couplings in histidine have rarely been reported. Here, we propose double spin-echo sequences to compare the observed signals with and without a 90° pulse between the two spin-echo periods, such that their signal ratio as a function of the echo time solely depends on homonuclear scalar couplings, allowing for measuring weak homonuclear scalar couplings without influence from transverse dephasing effects, thus capable of revealing hydrogen-bond mediated 15N-15N J -couplings that can provide direct and definitive evidence for the formation of N...H...N hydrogen-bonding associated with the imidazole ring. We used two 13C,15N labeled histidine samples recrystallized from solutions at pH 6.3 and pH 11.0 to demonstrate the feasibility of this method and reveal the existence of a weak two-bond scalar coupling between the N δ1 and N ε2 sites in the histidine imidazole ring in three tautomeric states and the presence of a hydrogen-bond mediated scalar coupling between the N δ1 site in the imidazole ring and the backbone N α site in the histidine neutral τ and π states. Our results demonstrate that weak 15N homonuclear scalar couplings can be measured even when their values are less than their corresponding intrinsic natural linewidths, thus providing direct and definitive evidence for the formation of N...H...N hydrogen bonding that is associated with the histidine imidazole ring. [ABSTRACT FROM AUTHOR]

Real-time band-selective homonuclear (1) H decoupling during data acquisition of z-filtered J-resolved spectroscopy produces (1) H-decoupled (1) H NMR spectra and leads to sensitivity enhancement and improved resolution, and thus aids the measurement of J couplings and residual dipolar couplings in crowded regions of (1) H NMR spectrum. High quality spectra from peptides, organic molecules, and also from enantiomers dissolved in weakly aligned chiral media are reported., (© 2015 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.)