177 results match your criteria Progress in nuclear magnetic resonance spectroscopy[Journal]


A quarter of a century of SERF: The progress of an NMR pulse sequence and its application.

Authors:
Stefan Berger

Prog Nucl Magn Reson Spectrosc 2018 10 28;108:74-114. Epub 2018 Nov 28.

Institute of Analytical Chemistry, University Leipzig, Johannisallee 29, D-04103 Leipzig, Germany. Electronic address:

SERF, an NMR pulse sequence for selectively measuring a spin coupling constant without interference from other couplings, was published by the current author almost 25 years ago in 1995. Since then, about 35 modifications and extensions of the original have been published by other groups and applied to many chemical problems. This review discusses these modifications and provides pertinent examples. Read More

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http://dx.doi.org/10.1016/j.pnmrs.2018.10.001DOI Listing
October 2018
1 Read

Theoretical calculations of carbon-hydrogen spin-spin coupling constants.

Authors:
Leonid B Krivdin

Prog Nucl Magn Reson Spectrosc 2018 10 13;108:17-73. Epub 2018 Oct 13.

A.E. Favorsky Irkutsk Institute of Chemistry, Siberian Branch of the Russian Academy of Sciences, Favorsky St. 1, 664033 Irkutsk, Russia. Electronic address:

Structural applications of theoretical calculations of carbon-hydrogen spin-spin coupling constants are reviewed covering papers published mainly during the last 10-15 years with a special emphasis on the most notable studies of hybridization, substitution and stereoelectronic effects together with the investigation of hydrogen bonding and intermolecular interactions. The wide scope of different applications of calculated carbon-hydrogen couplings in the structural elucidation of particular classes of organic and bioorganic molecules is reviewed, concentrating mainly on saturated, unsaturated, aromatic and heteroaromatic compounds and their functional derivatives, as well as on natural compounds and carbohydrates. The review is dedicated to Professor Emeritus Michael Barfield in view of his invaluable pioneering contribution to this field. Read More

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http://dx.doi.org/10.1016/j.pnmrs.2018.10.002DOI Listing
October 2018
1 Read

MR approaches in neurodegenerative disorders.

Authors:
Andrew M Blamire

Prog Nucl Magn Reson Spectrosc 2018 10 3;108:1-16. Epub 2018 Nov 3.

Institute of Cellular Medicine and Centre for In Vivo Imaging, Newcastle University, UK. Electronic address:

Neurodegenerative disease is the umbrella term which refers to a range of clinical conditions causing degeneration of neurons within the central nervous system leading to loss of brain function and eventual death. The most prevalent of these is Alzheimer's disease (AD), which affects approximately 50 million people worldwide and is predicted to reach 75 million by 2030. Neurodegenerative diseases can only be fully diagnosed at post mortem by neuropathological assessment of the type and distribution of protein deposits which characterise each different condition, but there is a clear role for imaging technologies in aiding patient diagnoses in life. Read More

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https://linkinghub.elsevier.com/retrieve/pii/S00796565183003
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http://dx.doi.org/10.1016/j.pnmrs.2018.11.001DOI Listing
October 2018
9 Reads

Characterization of intrinsically disordered proteins and their dynamic complexes: From in vitro to cell-like environments.

Prog Nucl Magn Reson Spectrosc 2018 12 31;109:79-100. Epub 2018 Jul 31.

Univ. Grenoble Alpes, CNRS, CEA, IBS, F-38000 Grenoble, France. Electronic address:

Over the last two decades, it has become increasingly clear that a large fraction of the human proteome is intrinsically disordered or contains disordered segments of significant length. These intrinsically disordered proteins (IDPs) play important regulatory roles throughout biology, underlining the importance of understanding their conformational behavior and interaction mechanisms at the molecular level. Here we review recent progress in the NMR characterization of the structure and dynamics of IDPs in various functional states and environments. Read More

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http://dx.doi.org/10.1016/j.pnmrs.2018.07.001DOI Listing
December 2018
1 Read

Structure determination of supra-molecular assemblies by solid-state NMR: Practical considerations.

Prog Nucl Magn Reson Spectrosc 2018 12 18;109:51-78. Epub 2018 Jun 18.

Department of Molecular Biophysics, Leibniz-Forschungsinstitut für Molekulare Pharmakologie (FMP), 13125 Berlin, Germany; Institut für Biologie, Humboldt-Universität zu Berlin, 10115 Berlin, Germany. Electronic address:

In the cellular environment, biomolecules assemble in large complexes which can act as molecular machines. Determining the structure of intact assemblies can reveal conformations and inter-molecular interactions that are only present in the context of the full assembly. Solid-state NMR (ssNMR) spectroscopy is a technique suitable for the study of samples with high molecular weight that allows the atomic structure determination of such large protein assemblies under nearly physiological conditions. Read More

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http://dx.doi.org/10.1016/j.pnmrs.2018.06.002DOI Listing
December 2018
1 Read

Recent advances in solid-state nuclear magnetic resonance spectroscopy of exotic nuclei.

Prog Nucl Magn Reson Spectrosc 2018 12 16;109:160-199. Epub 2018 Aug 16.

Department of Chemistry and Biomolecular Sciences & Centre for Catalysis Research and Innovation, University of Ottawa, 10 Marie Curie Private, Ottawa, Ontario K1N 6N5, Canada. Electronic address:

We present a review of recent advances in solid-state nuclear magnetic resonance (SSNMR) studies of exotic nuclei. Exotic nuclei may be spin-1/2 or quadrupolar, and typically have low gyromagnetic ratios, low natural abundances, large quadrupole moments (when I > 1/2), or some combination of these properties, generally resulting in low receptivities and/or prohibitively broad line widths. Some nuclides are little studied for other reasons, also rendering them somewhat exotic. Read More

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http://dx.doi.org/10.1016/j.pnmrs.2018.08.002DOI Listing
December 2018
1 Read

High-resolution methods for the measurement of scalar coupling constants.

Prog Nucl Magn Reson Spectrosc 2018 12 16;109:135-159. Epub 2018 Aug 16.

Russell H. Morgan Department of Radiology and Radiological Science, The Johns Hopkins University School of Medicine, Baltimore, MD 21287, USA; F. M. Kirby Center for Functional Brain Imaging, Kennedy Krieger Institute, Baltimore, MD 21205, USA.

Scalar couplings provide important information regarding molecular structure and dynamics. The measurement of scalar coupling constants constitutes a topic of interest and significance in NMR spectroscopy. However, the measurement of J values is often not straightforward because of complex signal splitting patterns and signal overlap. Read More

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http://dx.doi.org/10.1016/j.pnmrs.2018.08.003DOI Listing
December 2018
2 Reads

Spatial encoding and spatial selection methods in high-resolution NMR spectroscopy.

Prog Nucl Magn Reson Spectrosc 2018 12 3;109:101-134. Epub 2018 Aug 3.

Institut de Chimie des Substances Naturelles, CNRS UPR2301, Univ. Paris Sud, Université Paris-Saclay, Avenue de la Terrasse, 91190 Gif-sur-Yvette, France. Electronic address:

A family of high-resolution NMR methods share the common concept of acquiring in parallel different sub-experiments in different spatial regions of the NMR tube. These spatial encoding and spatial selection methods were for the most part introduced independently from each other and serve different purposes, but they share common ingredients, often derived from magnetic resonance imaging, and they all benefit from a greatly improved time-efficiency. This review article provides a description of several spatial encoding and spatial selection methods, including single-scan multidimensional experiments (ultrafast 2D NMR, DOSY, Z spectroscopy, inversion recovery and Laplace NMR), pure shift and selective refocusing experiments (including Zangger-Sterk decoupling, G-SERF and PSYCHE), a Z filter, and fast-pulsing slice-selective experiments. Read More

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http://dx.doi.org/10.1016/j.pnmrs.2018.08.001DOI Listing
December 2018
1 Read

Pros and cons of ultra-high-field MRI/MRS for human application.

Prog Nucl Magn Reson Spectrosc 2018 12 8;109:1-50. Epub 2018 Jun 8.

High-Field Magnetic Resonance Center, Max-Planck-Institute for Biological Cybernetics, Tübingen, Germany. Electronic address:

Magnetic resonance imaging and spectroscopic techniques are widely used in humans both for clinical diagnostic applications and in basic research areas such as cognitive neuroimaging. In recent years, new human MR systems have become available operating at static magnetic fields of 7 T or higher (≥300 MHz proton frequency). Imaging human-sized objects at such high frequencies presents several challenges including non-uniform radiofrequency fields, enhanced susceptibility artifacts, and higher radiofrequency energy deposition in the tissue. Read More

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http://dx.doi.org/10.1016/j.pnmrs.2018.06.001DOI Listing
December 2018
2 Reads

Carbon-carbon spin-spin coupling constants: Practical applications of theoretical calculations.

Authors:
Leonid B Krivdin

Prog Nucl Magn Reson Spectrosc 2018 04 3;105:54-99. Epub 2018 Mar 3.

A.E. Favorsky Irkutsk Institute of Chemistry, Siberian Branch of the Russian Academy of Sciences, Favorsky St. 1, 664033 Irkutsk, Russia. Electronic address:

Practical applications of theoretical calculations of carbon-carbon spin-spin coupling constants in particular classes of organic and bioorganic molecules are reviewed, concentrating mainly on saturated, unsaturated, aromatic and heteroaromatic compounds and their functional derivatives as well as on carbohydrates and natural compounds. Read More

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http://dx.doi.org/10.1016/j.pnmrs.2018.03.001DOI Listing
April 2018
4 Reads

Solution NMR of SNAREs, complexin and α-synuclein in association with membrane-mimetics.

Prog Nucl Magn Reson Spectrosc 2018 04 8;105:41-53. Epub 2018 Feb 8.

Center for Membrane and Cell Physiology and Department of Molecular Physiology and Biological Physics, University of Virginia School of Medicine, Charlottesville, VA 22908, USA.

SNARE-mediated membrane fusion is a ubiquitous process responsible for intracellular vesicle trafficking, including membrane fusion in exocytosis that leads to hormone and neurotransmitter release. The proteins that facilitate this process are highly dynamic and adopt multiple conformations when they interact with other proteins and lipids as they form highly regulated molecular machines that operate on membranes. Solution NMR is an ideal method to capture high-resolution glimpses of the molecular transformations that take place when these proteins come together and work on membranes. Read More

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http://dx.doi.org/10.1016/j.pnmrs.2018.02.001DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5863748PMC
April 2018
7 Reads

Multiparametric (mp) MRI of prostate cancer.

Prog Nucl Magn Reson Spectrosc 2018 04 31;105:23-40. Epub 2018 Jan 31.

Department of NMR & MRI Facility, All India Institute of Medical Sciences, Ansari Nagar, New Delhi 110029, India. Electronic address:

Prostate cancer (PCa) is one of the most prevalent cancers in men. A large number of men are detected with PCa; however, the clinical behavior ranges from low-grade indolent tumors that never develop into a clinically significant disease to aggressive, invasive tumors that may rapidly progress to metastatic disease. The challenges in clinical management of PCa are at levels of screening, diagnosis, treatment, and follow-up after treatment. Read More

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http://dx.doi.org/10.1016/j.pnmrs.2018.01.001DOI Listing
April 2018
5 Reads

Protein labeling strategies for liquid-state NMR spectroscopy using cell-free synthesis.

Prog Nucl Magn Reson Spectrosc 2018 04 7;105:1-22. Epub 2017 Dec 7.

Institute of Biophysical Chemistry and Center for Biomolecular Magnetic Resonance, Goethe University, Max-von-Laue Str. 9, 60438 Frankfurt, Germany. Electronic address:

Preparation of a protein sample for liquid-state nuclear magnetic resonance (NMR) spectroscopy analysis requires optimization of many parameters. This review describes labeling strategies for obtaining assignments of protein resonances. Particular emphasis is placed on the advantages of cell-free protein production, which enables exclusive labeling of the protein of interest, thereby simplifying downstream processing steps and increasing the availability of different labeling strategies for a target protein. Read More

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http://dx.doi.org/10.1016/j.pnmrs.2017.11.004DOI Listing
April 2018
6 Reads

Environmental metabolomics with data science for investigating ecosystem homeostasis.

Prog Nucl Magn Reson Spectrosc 2018 02 21;104:56-88. Epub 2017 Nov 21.

RIKEN Center for Sustainable Resource Science, 1-7-22 Suehiro-cho, Tsurumi-ku, Yokohama, Kanagawa 230-0045, Japan; Graduate School of Medical Life Science, Yokohama City University, 1-7-29 Suehiro-cho, Tsurumi-ku, Yokohama, Kanagawa 230-0045, Japan.

A natural ecosystem can be viewed as the interconnections between complex metabolic reactions and environments. Humans, a part of these ecosystems, and their activities strongly affect the environments. To account for human effects within ecosystems, understanding what benefits humans receive by facilitating the maintenance of environmental homeostasis is important. Read More

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http://dx.doi.org/10.1016/j.pnmrs.2017.11.003DOI Listing
February 2018
3 Reads

Multiscale nuclear magnetic relaxation dispersion of complex liquids in bulk and confinement.

Authors:
Jean-Pierre Korb

Prog Nucl Magn Reson Spectrosc 2018 02 10;104:12-55. Epub 2017 Nov 10.

Laboratoire de Physique de la Matière Condensée, Ecole Polytechnique, CNRS, Université de Paris Saclay, 91128 Palaiseau Cedex, France; Sorbonne Universités, UPMC Univ. Paris 06, CNRS, PHENIX Laboratory, F-75005 Paris, France. Electronic address:

The nuclear magnetic relaxation dispersion (NMRD) technique consists of measurement of the magnetic-field dependence of the longitudinal nuclear-spin-lattice relaxation rate 1/T. Usually, the acquisition of the NMRD profiles is made using a fast field cycling (FFC) NMR technique that varies the magnetic field and explores a very large range of Larmor frequencies (10 kHz < ω/(2π) <40 MHz). This allows extensive explorations of the fluctuations to which nuclear spin relaxation is sensitive. Read More

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http://dx.doi.org/10.1016/j.pnmrs.2017.11.001DOI Listing
February 2018
8 Reads

The NMR 'split peak effect' in cell suspensions: Historical perspective, explanation and applications.

Prog Nucl Magn Reson Spectrosc 2018 02 7;104:1-11. Epub 2017 Nov 7.

The University of Sydney, School of Life and Environmental Sciences, Faculty of Science, Sydney, NSW 2006, Australia; Australian National University, John Curtin School of Medical Research, College of Health and Medicine, Canberra, ACT 2601, Australia.

The physicochemical environment inside cells is distinctly different from that immediately outside. The selective exchange of ions, water and other molecules across the cell membrane, mediated by integral, membrane-embedded proteins is a hallmark of living systems. There are various methodologies available to measure the selectivity and rates (kinetics) of such exchange processes, including several that take advantage of the non-invasive nature of NMR spectroscopy. Read More

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http://dx.doi.org/10.1016/j.pnmrs.2017.11.002DOI Listing
February 2018
5 Reads

Calculation of N NMR chemical shifts: Recent advances and perspectives.

Authors:
Leonid B Krivdin

Prog Nucl Magn Reson Spectrosc 2017 11 24;102-103:98-119. Epub 2017 Aug 24.

A. E. Favorsky Irkutsk Institute of Chemistry, Siberian Branch of the Russian Academy of Sciences, Favorsky St. 1, 664033 Irkutsk, Russia. Electronic address:

Recent advances in computation of N NMR chemical shifts are reviewed, concentrating mainly on practical aspects of computational protocols and accuracy factors. The review includes the discussion of the level of theory, the choice of density functionals and basis sets together with taking into account solvent effects, rovibrational corrections and relativistic effects. Computational aspects of N NMR are illustrated for the series of neutral and protonated open-chain nitrogen-containing compounds and nitrogen heterocycles, coordination and intermolecular complexes. Read More

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http://dx.doi.org/10.1016/j.pnmrs.2017.08.001DOI Listing
November 2017
9 Reads

Plant metabolism as studied by NMR spectroscopy.

Prog Nucl Magn Reson Spectrosc 2017 11 8;102-103:61-97. Epub 2017 Jun 8.

Chimie et Interdisciplinarité: Synthèse, Analyse, Modélisation (CEISAM), UMR 6230, CNRS, Université de Nantes, Faculté des Sciences, BP 92208, 2 rue de la Houssinière, F-44322 Nantes Cedex 03, France; Institut Universitaire de France, 1 rue Descartes, 75005 Paris, France. Electronic address:

The study of plant metabolism impacts a broad range of domains such as plant cultural practices, plant breeding, human or animal nutrition, phytochemistry and green biotechnologies. Plant metabolites are extremely diverse in terms of structure or compound families as well as concentrations. This review attempts to illustrate how NMR spectroscopy, with its broad variety of experimental approaches, has contributed widely to the study of plant primary or specialized metabolism in very diverse ways. Read More

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http://dx.doi.org/10.1016/j.pnmrs.2017.05.001DOI Listing
November 2017
11 Reads

Atomic resolution conformational dynamics of intrinsically disordered proteins from NMR spin relaxation.

Prog Nucl Magn Reson Spectrosc 2017 11 10;102-103:43-60. Epub 2017 Jul 10.

Institut de Biologie Structurale (IBS), CEA, CNRS, University Grenoble Alpes, Grenoble 38044, France. Electronic address:

Nuclear magnetic resonance (NMR) spectroscopy is one of the most powerful experimental approaches for investigating the conformational behaviour of intrinsically disordered proteins (IDPs). IDPs represent a significant fraction of all proteomes, and, despite their importance for understanding fundamental biological processes, the molecular basis of their activity still remains largely unknown. The functional mechanisms exploited by IDPs in their interactions with other biomolecules are defined by their intrinsic dynamic modes and associated timescales, justifying the considerable interest over recent years in the development of technologies adapted to measure and describe this behaviour. Read More

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http://dx.doi.org/10.1016/j.pnmrs.2017.06.001DOI Listing
November 2017
8 Reads

Biomolecular MRI reporters: Evolution of new mechanisms.

Prog Nucl Magn Reson Spectrosc 2017 11 3;102-103:32-42. Epub 2017 Jun 3.

Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125, USA. Electronic address:

Magnetic resonance imaging (MRI) is a powerful technique for observing the function of specific cells and molecules inside living organisms. However, compared to optical microscopy, in which fluorescent protein reporters are available to visualize hundreds of cellular functions ranging from gene expression and chemical signaling to biomechanics, to date relatively few such reporters are available for MRI. Efforts to develop MRI-detectable biomolecules have mainly focused on proteins transporting paramagnetic metals for T and T relaxation enhancement or containing large numbers of exchangeable protons for chemical exchange saturation transfer. Read More

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http://dx.doi.org/10.1016/j.pnmrs.2017.05.002DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5726449PMC
November 2017
5 Reads

Monitoring protein folding through high pressure NMR spectroscopy.

Prog Nucl Magn Reson Spectrosc 2017 11 2;102-103:15-31. Epub 2017 Jun 2.

Centre de Biochimie Structural INSERM U1054, CNRS UMMR 5058, Université de Montpellier, Montpellier 34090, France. Electronic address:

High-pressure is a well-known perturbation method used to destabilize globular proteins. It is perfectly reversible, which is essential for a proper thermodynamic characterization of a protein equilibrium. In contrast to other perturbation methods such as heat or chemical denaturant that destabilize protein structures uniformly, pressure exerts local effects on regions or domains of a protein containing internal cavities. Read More

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http://dx.doi.org/10.1016/j.pnmrs.2017.05.003DOI Listing
November 2017
11 Reads

Dynamic nuclear polarization for sensitivity enhancement in modern solid-state NMR.

Prog Nucl Magn Reson Spectrosc 2017 11 23;102-103:120-195. Epub 2017 Jul 23.

Institute of Physical and Theoretical Chemistry, Institute of Biophysical Chemistry, and Center for Biomolecular Magnetic Resonance (BMRZ), Goethe University Frankfurt, Max-von-Laue-Str. 7-9, 60438 Frankfurt, Germany. Electronic address:

The field of dynamic nuclear polarization has undergone tremendous developments and diversification since its inception more than 6 decades ago. In this review we provide an in-depth overview of the relevant topics involved in DNP-enhanced MAS NMR spectroscopy. This includes the theoretical description of DNP mechanisms as well as of the polarization transfer pathways that can lead to a uniform or selective spreading of polarization between nuclear spins. Read More

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http://dx.doi.org/10.1016/j.pnmrs.2017.06.002DOI Listing
November 2017
4 Reads

NMR-based pharmacometabonomics: A new paradigm for personalised or precision medicine.

Authors:
Jeremy R Everett

Prog Nucl Magn Reson Spectrosc 2017 11 6;102-103:1-14. Epub 2017 May 6.

Medway Metabonomics Group, University of Greenwich, Chatham Maritime, Kent ME4 4TB, UK. Electronic address:

Metabolic profiling by NMR spectroscopy or hyphenated mass spectrometry, known as metabonomics or metabolomics, is an important tool for systems-based approaches in biology and medicine. The experiments are typically done in a diagnostic fashion where changes in metabolite profiles are interpreted as a consequence of an intervention or event; be that a change in diet, the administration of a drug, physical exertion or the onset of a disease. By contrast, pharmacometabonomics takes a prognostic approach to metabolic profiling, in order to predict the effects of drug dosing before it occurs. Read More

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http://dx.doi.org/10.1016/j.pnmrs.2017.04.003DOI Listing
November 2017
4 Reads

Recent advances in parallel imaging for MRI.

Prog Nucl Magn Reson Spectrosc 2017 08 2;101:71-95. Epub 2017 May 2.

Biomedical Engineering, Case Western Reserve University, Cleveland, OH, USA; Radiology, University Hospitals Cleveland Medical Center, Cleveland, OH, USA. Electronic address:

Magnetic Resonance Imaging (MRI) is an essential technology in modern medicine. However, one of its main drawbacks is the long scan time needed to localize the MR signal in space to generate an image. This review article summarizes some basic principles and recent developments in parallel imaging, a class of image reconstruction techniques for shortening scan time. Read More

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http://dx.doi.org/10.1016/j.pnmrs.2017.04.002DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5927614PMC
August 2017
5 Reads

MRI of chemical reactions and processes.

Prog Nucl Magn Reson Spectrosc 2017 08 30;101:51-70. Epub 2017 Mar 30.

School of Chemistry, University of Birmingham, Birmingham B15 2TT, UK.

As magnetic resonance imaging (MRI) can spatially resolve a wealth of molecular information available from nuclear magnetic resonance (NMR), it is able to non-invasively visualise the composition, properties and reactions of a broad range of spatially-heterogeneous molecular systems. Hence, MRI is increasingly finding applications in the study of chemical reactions and processes in a diverse range of environments and technologies. This article will explain the basic principles of MRI and how it can be used to visualise chemical composition and molecular properties, providing an overview of the variety of information available. Read More

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http://dx.doi.org/10.1016/j.pnmrs.2017.03.001DOI Listing
August 2017
5 Reads

Self-diffusion studies by intra- and inter-molecular spin-lattice relaxometry using field-cycling: Liquids, plastic crystals, porous media, and polymer segments.

Prog Nucl Magn Reson Spectrosc 2017 08 9;101:18-50. Epub 2017 Apr 9.

Institute of Physics, Kazan Federal University, Kazan 420008 Tatarstan, Russia.

Field-cycling NMR relaxometry is a well-established technique for probing molecular dynamics in a frequency range from typically a few kHz up to several tens of MHz. For the interpretation of relaxometry data, it is quite often assumed that the spin-lattice relaxation process is of an intra-molecular nature so that rotational fluctuations dominate. However, dipolar interactions as the main type of couplings between protons and other dipolar species without quadrupole moments can imply appreciable inter-molecular contributions. Read More

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http://dx.doi.org/10.1016/j.pnmrs.2017.04.001DOI Listing
August 2017
6 Reads

Static solid-state H NMR methods in studies of protein side-chain dynamics.

Prog Nucl Magn Reson Spectrosc 2017 08 14;101:1-17. Epub 2017 Mar 14.

University of Colorado Denver, Denver, CO 80204, USA.

In this review, we discuss the experimental static deuteron NMR techniques and computational approaches most useful for the investigation of side-chain dynamics in protein systems. Focus is placed on the interpretation of line shape and relaxation data within the framework of motional modeling. We consider both jump and diffusion models and apply them to uncover glassy behaviors, conformational exchange and dynamical transitions in proteins. Read More

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http://dx.doi.org/10.1016/j.pnmrs.2017.02.001DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5576518PMC
August 2017
7 Reads

Protein folding by NMR.

Prog Nucl Magn Reson Spectrosc 2017 05 9;100:52-77. Epub 2016 Nov 9.

Department of Molecular Biology and Biophysics, University of Connecticut Health Center, Farmington, CT 06030, USA. Electronic address:

Protein folding is a highly complex process proceeding through a number of disordered and partially folded nonnative states with various degrees of structural organization. These transiently and sparsely populated species on the protein folding energy landscape play crucial roles in driving folding toward the native conformation, yet some of these nonnative states may also serve as precursors for protein misfolding and aggregation associated with a range of devastating diseases, including neuro-degeneration, diabetes and cancer. Therefore, in vivo protein folding is often reshaped co- and post-translationally through interactions with the ribosome, molecular chaperones and/or other cellular components. Read More

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http://dx.doi.org/10.1016/j.pnmrs.2016.10.002DOI Listing
May 2017
7 Reads

Advanced solid-state NMR spectroscopy of natural organic matter.

Prog Nucl Magn Reson Spectrosc 2017 05 5;100:17-51. Epub 2017 Jan 5.

Department of Chemistry, Brandeis University, 415 South Street, Waltham, MA 02453, United States. Electronic address:

Solid-state NMR is essential for the characterization of natural organic matter (NOM) and is gaining importance in geosciences and environmental sciences. This review is intended to highlight advanced solid-state NMR techniques, especially a systematic approach to NOM characterization, and their applications to the study of NOM. We discuss some basics of how to acquire high-quality and quantitative solid-state C NMR spectra, and address some common technical mistakes that lead to unreliable spectra of NOM. Read More

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http://dx.doi.org/10.1016/j.pnmrs.2016.11.003DOI Listing
May 2017
4 Reads

Beyond the paradigm: Combining mass spectrometry and nuclear magnetic resonance for metabolomics.

Prog Nucl Magn Reson Spectrosc 2017 05 11;100:1-16. Epub 2017 Jan 11.

Department of Chemistry, University of Nebraska-Lincoln, Lincoln, NE 68588-0304, United States. Electronic address:

Metabolomics is undergoing tremendous growth and is being employed to solve a diversity of biological problems from environmental issues to the identification of biomarkers for human diseases. Nuclear magnetic resonance (NMR) and mass spectrometry (MS) are the analytical tools that are routinely, but separately, used to obtain metabolomics data sets due to their versatility, accessibility, and unique strengths. NMR requires minimal sample handling without the need for chromatography, is easily quantitative, and provides multiple means of metabolite identification, but is limited to detecting the most abundant metabolites (⩾1μM). Read More

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http://dx.doi.org/10.1016/j.pnmrs.2017.01.001DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5448308PMC
May 2017
8 Reads

Single-spin magnetic resonance in the nitrogen-vacancy center of diamond.

Prog Nucl Magn Reson Spectrosc 2017 02 26;98-99:50-62. Epub 2016 Dec 26.

Institut für Quantenoptik, Universität Ulm, Ulm, Germany.

Magnetic resonance of single spins has flourished mostly because of the unique properties of the NV center in diamond. This review covers the basic physics of this defect center, introduces the techniques for working with single spins and gives an overview of some applications like quantum information and sensing. Read More

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http://dx.doi.org/10.1016/j.pnmrs.2016.12.001DOI Listing
February 2017
3 Reads

Pseudocontact shifts in biomolecular NMR using paramagnetic metal tags.

Prog Nucl Magn Reson Spectrosc 2017 02 1;98-99:20-49. Epub 2016 Dec 1.

Australian National University, Research School of Chemistry, Canberra, ACT 2601, Australia. Electronic address: http://www.rsc.anu.edu.au/~go/index.html.

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http://dx.doi.org/10.1016/j.pnmrs.2016.11.001DOI Listing
February 2017
15 Reads

Singlet NMR methodology in two-spin-1/2 systems.

Authors:
Giuseppe Pileio

Prog Nucl Magn Reson Spectrosc 2017 02 1;98-99:1-19. Epub 2016 Dec 1.

Department of Chemistry, University of Southampton, SO17 1BJ, UK. Electronic address:

This paper discusses methodology developed over the past 12years in order to access and manipulate singlet order in systems comprising two coupled spin-1/2 nuclei in liquid-state nuclear magnetic resonance. Pulse sequences that are valid for different regimes are discussed, and fully analytical proofs are given using different spin dynamics techniques that include product operator methods, the single transition operator formalism, and average Hamiltonian theory. Methods used to filter singlet order from byproducts of pulse sequences are also listed and discussed analytically. Read More

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http://dx.doi.org/10.1016/j.pnmrs.2016.11.002DOI Listing
February 2017
2 Reads

NMR in drug discovery: A practical guide to identification and validation of ligands interacting with biological macromolecules.

Prog Nucl Magn Reson Spectrosc 2016 11 30;97:82-125. Epub 2016 Sep 30.

Novartis Institutes for BioMedical Research, Novartis Campus, 4002 Basel, Switzerland.

Protein-ligand interactions are at the heart of drug discovery research. NMR spectroscopy is an excellent technology to identify and validate protein-ligand interactions. A plethora of NMR methods are available which are powerful, robust and information-rich, but also have pitfalls and limitations. Read More

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http://dx.doi.org/10.1016/j.pnmrs.2016.09.001DOI Listing
November 2016
54 Reads

NMR solution structure determination of large RNA-protein complexes.

Prog Nucl Magn Reson Spectrosc 2016 11 27;97:57-81. Epub 2016 Oct 27.

Central European Institute of Technology, Masaryk University, Kamenice 753/5, 62500 Brno, Czech Republic. Electronic address:

Structure determination of RNA-protein complexes is essential for our understanding of the multiple layers of RNA-mediated posttranscriptional regulation of gene expression. Over the past 20years, NMR spectroscopy became a key tool for structural studies of RNA-protein interactions. Here, we review the progress being made in NMR structure determination of large ribonucleoprotein assemblies. Read More

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http://dx.doi.org/10.1016/j.pnmrs.2016.10.001DOI Listing
November 2016
9 Reads
2 Citations
7.240 Impact Factor

Detection of intermolecular NOE interactions in large protein complexes.

Prog Nucl Magn Reson Spectrosc 2016 11 18;97:40-56. Epub 2016 Aug 18.

Department of Chemistry and Macromolecular Assembly Institute, College of Staten Island of the City University of New York, Staten Island, New York 10314, USA; Biochemistry and Chemistry, The Graduate Center of the City University of New York, New York, NY 10016, USA; Department of Structural Biology, Weizmann Institute of Science, Rehovot 76100, Israel(1).

Intermolecular NOE interactions are invaluable for structure determination of biomolecular complexes by NMR and they represent the "gold-standard" amongst NMR measurements for characterizing interfaces. These NOEs constitute only a small fraction of the observed NOEs in a complex and are usually weaker than many of the intramolecular NOEs. A number of methods have been developed to remove the intramolecular NOEs that interfere with the identification of intermolecular NOEs. Read More

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http://dx.doi.org/10.1016/j.pnmrs.2016.08.002DOI Listing
November 2016
11 Reads

Five decades of homonuclear dipolar decoupling in solid-state NMR: Status and outlook.

Prog Nucl Magn Reson Spectrosc 2016 11 4;97:1-39. Epub 2016 Aug 4.

TIFR Centre for Interdisciplinary Sciences, Tata Institute of Fundamental Research, 21 Brundavan Colony, Narsingi, Hyderabad 500 075, India; Department of Chemical Sciences, Tata Institute of Fundamental Research, Homi Bhabha Road, Colaba, Mumbai 400 005, India.

It has been slightly more than fifty years since the first homonuclear spin decoupling scheme, Lee-Goldburg decoupling, was proposed for removing homonuclear dipolar interactions in solid-state nuclear magnetic resonance. A family of such schemes has made observation of high-resolution NMR spectra of abundant spins possible in various applications in solid state. This review outlines the strategies used in this field and the future prospects of homonuclear spin decoupling in solid-state NMR. Read More

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http://dx.doi.org/10.1016/j.pnmrs.2016.08.001DOI Listing
November 2016
3 Reads

Stable isotope labeling methods for DNA.

Prog Nucl Magn Reson Spectrosc 2016 08 20;96:89-108. Epub 2016 Jun 20.

Institute for Molecules and Materials, Radboud University, 6525 AJ Nijmegen, The Netherlands. Electronic address:

NMR is a powerful method for studying proteins and nucleic acids in solution. The study of nucleic acids by NMR is far more challenging than for proteins, which is mainly due to the limited number of building blocks and unfavorable spectral properties. For NMR studies of DNA molecules, (site specific) isotope enrichment is required to facilitate specific NMR experiments and applications. Read More

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http://dx.doi.org/10.1016/j.pnmrs.2016.06.001DOI Listing
August 2016
3 Reads

Conformational analysis of small molecules: NMR and quantum mechanics calculations.

Prog Nucl Magn Reson Spectrosc 2016 08 22;96:73-88. Epub 2016 Apr 22.

Institute of Chemistry, University of Campinas, PO Box 6154, 13083-970 Campinas, Sao Paulo, Brazil. Electronic address:

This review deals with conformational analysis in small organic molecules, and describes the stereoelectronic interactions responsible for conformational stability. Conformational analysis is usually performed using NMR spectroscopy through measurement of coupling constants at room or low temperature in different solvents to determine the populations of conformers in solution. Quantum mechanical calculations are used to address the interactions responsible for conformer stability. Read More

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http://dx.doi.org/10.1016/j.pnmrs.2016.04.001DOI Listing
August 2016
5 Reads

Assessment of dietary exposure and effect in humans: The role of NMR.

Prog Nucl Magn Reson Spectrosc 2016 08 6;96:58-72. Epub 2016 Apr 6.

Unilever R&D Vlaardingen, Olivier van Noortlaan 120, 3130AC Vlaardingen, The Netherlands.

In human nutritional science progress has always depended strongly on analytical measurements for establishing relationships between diet and health. This field has undergone significant changes as a result of the development of NMR and mass spectrometry methods for large scale detection, identification and quantification of metabolites in body fluids. This has allowed systematic studies of the metabolic fingerprints that biological processes leave behind, and has become the research field of metabolomics. Read More

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http://dx.doi.org/10.1016/j.pnmrs.2016.03.001DOI Listing
August 2016
6 Reads

Quantitative analysis of protein-ligand interactions by NMR.

Prog Nucl Magn Reson Spectrosc 2016 08 3;96:47-57. Epub 2016 Mar 3.

Bioorganic Research Institute, Suntory Foundation for Life Sciences, 1-1-1 Wakayamadai, Shimamoto, Mishima, Osaka 618-8503, Japan; Department of Molecular Engineering, Graduate School of Engineering, Kyoto University, Kyoto-Daigaku Katsura, Nishikyo-Ku, Kyoto 615-8510, Japan. Electronic address:

Protein-ligand interactions have been commonly studied through static structures of the protein-ligand complex. Recently, however, there has been increasing interest in investigating the dynamics of protein-ligand interactions both for fundamental understanding of the underlying mechanisms and for drug development. NMR is a versatile and powerful tool, especially because it provides site-specific quantitative information. Read More

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http://dx.doi.org/10.1016/j.pnmrs.2016.02.002DOI Listing
August 2016
4 Reads

"Pulse pair technique in high resolution NMR" a reprint of the historical 1971 lecture notes on two-dimensional spectroscopy.

Prog Nucl Magn Reson Spectrosc 2016 05 12;94-95:75-80. Epub 2016 Apr 12.

Faculty of Sciences, University of Brussels (ULB and VUB), Brussels, Belgium.

The review articles published in "Progress in NMR Spectroscopy" are usually invited treatments of topics of current interest, but occasionally the Editorial Board may take an initiative to publish important historical material that is not widely available. The present article represents just such a case. Jean Jeener gave a lecture in 1971 at a summer school in Basko Polje, in what was then called Yugoslavia. Read More

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https://linkinghub.elsevier.com/retrieve/pii/S00796565163000
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http://dx.doi.org/10.1016/j.pnmrs.2016.03.002DOI Listing
May 2016
5 Reads

Deuterium NMR investigations of field-induced director alignment in nematic liquid crystals.

Prog Nucl Magn Reson Spectrosc 2016 05 2;94-95:37-74. Epub 2016 Feb 2.

Chemistry, University of Southampton, Highfield, Southampton SO17 1BJ, United Kingdom.

There have been many investigations of the alignment of nematic liquid crystals by either a magnetic and/or an electric field. The basic features of the important hydrodynamic processes for low molar mass nematics have been characterized for the systems in their equilibrium and non-equilibrium states. These have been created using electric and magnetic fields to align the director and deuterium nuclear magnetic resonance ((2)H NMR) spectroscopy has been used to explore this alignment. Read More

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http://dx.doi.org/10.1016/j.pnmrs.2016.01.002DOI Listing
May 2016
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Recent advances in application of (27)Al NMR spectroscopy to materials science.

Prog Nucl Magn Reson Spectrosc 2016 05 10;94-95:11-36. Epub 2016 Feb 10.

Institut Lavoisier de Versailles (UMR CNRS 8180), Tectospin Group, Université de Versailles Saint Quentin en Yvelines, 78035 Versailles, France.

Valuable information about the local environment of the aluminum nucleus can be obtained through (27)Al Nuclear Magnetic Resonance (NMR) parameters like the isotropic chemical shift, scalar and quadrupolar coupling constants, and relaxation rate. With nearly 250 scientific articles per year dealing with (27)Al NMR spectroscopy, this analytical tool has become popular because of the recent progress that has made the acquisition and interpretation of the NMR data much easier. The application of (27)Al NMR techniques to various classes of compounds, either in solution or solid-state, has been shown to be extremely informative concerning local structure and chemistry of aluminum in its various environments. Read More

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http://dx.doi.org/10.1016/j.pnmrs.2016.01.003DOI Listing
May 2016
4 Reads

Diffusion NMR studies of macromolecular complex formation, crowding and confinement in soft materials.

Prog Nucl Magn Reson Spectrosc 2016 05 4;94-95:1-10. Epub 2016 Feb 4.

Department of Physics and Physical Oceanography, Memorial University, St. John's, Newfoundland and Labrador, Canada.

Label-free methods to obtain hydrodynamic size from diffusion measurements are desirable in environments that contain multiple macromolecular species at a high total concentration: one example is the crowded cellular environment. In complex, multi-species macromolecular environments - in this article, we feature aqueous systems involving polymers, surfactants and proteins - the link between dynamics and size is harder to unpack due to macromolecular crowding and confinement. In this review, we demonstrate that the pulsed-field gradient NMR technique, with its spectral separation of different chemical components, is ideal for studying the dynamics of the entire system simultaneously and without labelling, in a wide range of systems. Read More

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http://dx.doi.org/10.1016/j.pnmrs.2016.01.004DOI Listing
May 2016
4 Reads

Studying Dynamics by Magic-Angle Spinning Solid-State NMR Spectroscopy: Principles and Applications to Biomolecules.

Prog Nucl Magn Reson Spectrosc 2016 08 15;96:1-46. Epub 2016 Feb 15.

ETH Zürich, Physical Chemistry, Vladimir-Prelog-Weg 2, 8093 Zürich, Switzerland.

Magic-angle spinning solid-state NMR spectroscopy is an important technique to study molecular structure, dynamics and interactions, and is rapidly gaining importance in biomolecular sciences. Here we provide an overview of experimental approaches to study molecular dynamics by MAS solid-state NMR, with an emphasis on the underlying theoretical concepts and differences of MAS solid-state NMR compared to solution-state NMR. The theoretical foundations of nuclear spin relaxation are revisited, focusing on the particularities of spin relaxation in solid samples under magic-angle spinning. Read More

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http://dx.doi.org/10.1016/j.pnmrs.2016.02.001DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4836562PMC
August 2016
5 Reads

How to tackle protein structural data from solution and solid state: An integrated approach.

Prog Nucl Magn Reson Spectrosc 2016 Feb 21;92-93:54-70. Epub 2016 Jan 21.

Magnetic Resonance Center (CERM) and Department of Chemistry "Ugo Schiff", University of Florence, Italy(1). Electronic address:

Long-range NMR restraints, such as diamagnetic residual dipolar couplings and paramagnetic data, can be used to determine 3D structures of macromolecules. They are also used to monitor, and potentially to improve, the accuracy of a macromolecular structure in solution by validating or "correcting" a crystal model. Since crystal structures suffer from crystal packing forces they may not be accurate models for the macromolecular structures in solution. Read More

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http://dx.doi.org/10.1016/j.pnmrs.2016.01.001DOI Listing
February 2016
23 Reads

Applications of NMR spectroscopy to systems biochemistry.

Prog Nucl Magn Reson Spectrosc 2016 Feb 6;92-93:18-53. Epub 2016 Feb 6.

Department of Toxicology and Cancer Biology, University of Kentucky, 789 S. Limestone St., Lexington, KY 40536, United States. Electronic address:

The past decades of advancements in NMR have made it a very powerful tool for metabolic research. Despite its limitations in sensitivity relative to mass spectrometric techniques, NMR has a number of unparalleled advantages for metabolic studies, most notably the rigor and versatility in structure elucidation, isotope-filtered selection of molecules, and analysis of positional isotopomer distributions in complex mixtures afforded by multinuclear and multidimensional experiments. In addition, NMR has the capacity for spatially selective in vivo imaging and dynamical analysis of metabolism in tissues of living organisms. Read More

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http://dx.doi.org/10.1016/j.pnmrs.2016.01.005DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4850081PMC
February 2016
8 Reads