Progress in Nuclear Magnetic Resonance Spectroscopy最新文献

{"title":"NMR application in unconventional shale reservoirs – A new porous media research frontier","authors":"Yi-Qiao Song,&nbsp;Ravinath Kausik","doi":"10.1016/j.pnmrs.2019.03.002","DOIUrl":"10.1016/j.pnmrs.2019.03.002","url":null,"abstract":"<div><p>Unconventional shale reservoirs have greatly contributed to the recent surge in petroleum production in the United States and are expected to lead the US oil production to a historical high in 2018. The complexity of the rocks and fluids in these reservoirs presents a significant challenge to the traditional approaches to the evaluation of geological formations due to the low porosity, permeability, complex lithology and fluid composition. NMR has emerged as the key measurement for evaluating these reservoirs, for quantifying their petrophysical parameters, fluid properties, and determining productivity. Measurement of the <span><math><mrow><msub><mrow><mi>T</mi></mrow><mrow><mn>1</mn></mrow></msub><mo>/</mo><msub><mrow><mi>T</mi></mrow><mrow><mn>2</mn></mrow></msub></mrow></math></span> ratio by 2D NMR has been found to be critical for identifying the fluid composition of kerogen, bitumen, light/heavy oils, gases and brine in these formations. This paper will first provide a brief review of the theories of relaxation, measurement methods, and data inversion techniques and then will discuss several examples of applications of these NMR methods for understanding various aspects of the unconventional reservoirs. At the end, we will briefly discuss a few other topics, which are still in their developmental stages, such as solid state NMR, and their potential applications for shale rock evaluation.</p></div>","PeriodicalId":20740,"journal":{"name":"Progress in Nuclear Magnetic Resonance Spectroscopy","volume":"112 ","pages":"Pages 17-33"},"PeriodicalIF":6.1,"publicationDate":"2019-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.pnmrs.2019.03.002","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"42544258","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Paramagnetic NMR in solution and the solid state","authors":"Andrew J. Pell ,&nbsp;Guido Pintacuda ,&nbsp;Clare P. Grey","doi":"10.1016/j.pnmrs.2018.05.001","DOIUrl":"10.1016/j.pnmrs.2018.05.001","url":null,"abstract":"<div><p>The field of paramagnetic NMR has expanded considerably in recent years. This review addresses both the theoretical description of paramagnetic NMR, and the way in which it is currently practised. We provide a review of the theory of the NMR parameters of systems in both solution and the solid state. Here we unify the different languages used by the NMR, EPR, quantum chemistry/DFT, and magnetism communities to provide a comprehensive and coherent theoretical description. We cover the theory of the paramagnetic shift and shift anisotropy in solution both in the traditional formalism in terms of the magnetic susceptibility tensor, and using a more modern formalism employing the relevant EPR parameters, such as are used in first-principles calculations. In addition we examine the theory first in the simple non-relativistic picture, and then in the presence of spin-orbit coupling. These ideas are then extended to a description of the paramagnetic shift in periodic solids, where it is necessary to include the bulk magnetic properties, such as magnetic ordering at low temperatures. The description of the paramagnetic shift is completed by describing the current understanding of such shifts due to lanthanide and actinide ions. We then examine the paramagnetic relaxation enhancement, using a simple model employing a phenomenological picture of the electronic relaxation, and again using a more complex state-of-the-art theory which incorporates electronic relaxation explicitly. An additional important consideration in the solid state is the impact of bulk magnetic susceptibility effects on the form of the spectrum, where we include some ideas from the field of classical electrodynamics. We then continue by describing in detail the solution and solid-state NMR methods that have been deployed in the study of paramagnetic systems in chemistry, biology, and the materials sciences. Finally we describe a number of case studies in paramagnetic NMR that have been specifically chosen to highlight how the theory in part one, and the methods in part two, can be used in practice. The systems chosen include small organometallic complexes in solution, solid battery electrode materials, metalloproteins in both solution and the solid state, systems containing lanthanide ions, and multi-component materials used in pharmaceutical controlled-release formulations that have been doped with paramagnetic species to measure the component domain sizes.</p></div>","PeriodicalId":20740,"journal":{"name":"Progress in Nuclear Magnetic Resonance Spectroscopy","volume":"111 ","pages":"Pages 1-271"},"PeriodicalIF":6.1,"publicationDate":"2019-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.pnmrs.2018.05.001","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"37290327","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Protein sample preparation for solid-state NMR investigations","authors":"Denis Lacabanne ,&nbsp;Marie-Laure Fogeron ,&nbsp;Thomas Wiegand ,&nbsp;Riccardo Cadalbert ,&nbsp;Beat H. Meier ,&nbsp;Anja Böckmann","doi":"10.1016/j.pnmrs.2019.01.001","DOIUrl":"10.1016/j.pnmrs.2019.01.001","url":null,"abstract":"<div><p>Preparation of a protein sample for solid-state NMR is in many aspects similar to solution-state NMR approaches, mainly with respect to the need for stable isotope labeling. But the possibility of using solid-state NMR to investigate membrane proteins in (native) lipids adds the important requirement of adapted membrane-reconstitution schemes. Also, dynamic nuclear polarization and paramagnetic NMR in solids need specific schemes using metal ions and radicals. Sample sedimentation has enabled structural investigations of objects inaccessible to other structural techniques, but rotor filling using sedimentation has become increasingly complex with smaller and smaller rotors, as needed for higher and higher magic-angle spinning (MAS) frequencies. Furthermore, solid-state NMR can investigate very large proteins and their complexes without the concomitant increase in line widths, motivating the use of selective labeling and unlabeling strategies, as well as segmental labeling, to decongest spectra. The possibility of investigating sub-milligram amounts of protein today using advanced fast MAS techniques enables alternative protein synthesis schemes such as cell-free expression. Here we review these specific aspects of solid-state NMR sample preparation.</p></div>","PeriodicalId":20740,"journal":{"name":"Progress in Nuclear Magnetic Resonance Spectroscopy","volume":"110 ","pages":"Pages 20-33"},"PeriodicalIF":6.1,"publicationDate":"2019-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.pnmrs.2019.01.001","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"36998191","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Magnetic resonance thermometry and its biological applications – Physical principles and practical considerations","authors":"Henrik Odéen,&nbsp;Dennis L. Parker","doi":"10.1016/j.pnmrs.2019.01.003","DOIUrl":"10.1016/j.pnmrs.2019.01.003","url":null,"abstract":"<div><p>Most parameters that influence the magnetic resonance imaging (MRI) signal experience a temperature dependence. The fact that MRI can be used for non-invasive measurements of temperature and temperature change deep inside the human body has been known for over 30 years. Today, MR temperature imaging is widely used to monitor and evaluate thermal therapies such as radio frequency, microwave, laser, and focused ultrasound therapy. In this paper we cover the physical principles underlying the biological applications of MR temperature imaging and discuss practical considerations and remaining challenges. For biological tissue, the MR signal of interest comes mostly from hydrogen protons of water molecules but also from protons in, e.g., adipose tissue and various metabolites. Most of the discussed methods, such as those using the proton resonance frequency (PRF) shift, T₁, T₂, and diffusion only measure temperature change, but measurements of absolute temperatures are also possible using spectroscopic imaging methods (taking advantage of various metabolite signals as internal references) or various types of contrast agents. Currently, the PRF method is the most used clinically due to good sensitivity, excellent linearity with temperature, and because it is largely independent of tissue type. Because the PRF method does not work in adipose tissues, T₁- and T₂-based methods have recently gained interest for monitoring temperature change in areas with high fat content such as the breast and abdomen. Absolute temperature measurement methods using spectroscopic imaging and contrast agents often offer too low spatial and temporal resolution for accurate monitoring of ablative thermal procedures, but have shown great promise in monitoring the slower and usually less spatially localized temperature change observed during hyperthermia procedures. Much of the current research effort for ablative procedures is aimed at providing faster measurements, larger field-of-view coverage, simultaneous monitoring in aqueous and adipose tissues, and more motion-insensitive acquisitions for better precision measurements in organs such as the heart, liver, and kidneys. For hyperthermia applications, larger coverage, motion insensitivity, and simultaneous aqueous and adipose monitoring are also important, but great effort is also aimed at solving the problem of long-term field drift which gets interpreted as temperature change when using the PRF method.</p></div>","PeriodicalId":20740,"journal":{"name":"Progress in Nuclear Magnetic Resonance Spectroscopy","volume":"110 ","pages":"Pages 34-61"},"PeriodicalIF":6.1,"publicationDate":"2019-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.pnmrs.2019.01.003","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"36998194","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Unspinning chromatin: Revealing the dynamic nucleosome landscape by NMR","authors":"Clara L. van Emmerik,&nbsp;Hugo van Ingen","doi":"10.1016/j.pnmrs.2019.01.002","DOIUrl":"10.1016/j.pnmrs.2019.01.002","url":null,"abstract":"<div><p>NMR is an essential technique for obtaining information at atomic resolution on the structure, motions and interactions of biomolecules. Here, we review the contribution of NMR to our understanding of the fundamental unit of chromatin: the nucleosome. Nucleosomes compact the genome by wrapping the DNA around a protein core, the histone octamer, thereby protecting genomic integrity. Crucially, the imposed barrier also allows strict regulation of gene expression, DNA replication and DNA repair processes through an intricate system of histone and DNA modifications and a wide range of interactions between nucleosomes and chromatin factors. In this review, we describe how NMR has contributed to deciphering the molecular basis of nucleosome function. Starting from pioneering studies in the 1960s using natural abundance NMR studies, we focus on the progress in sample preparation and NMR methodology that has allowed high-resolution studies on the nucleosome and its subunits. We summarize the results and approaches of state-of-the-art NMR studies on nucleosomal DNA, histone complexes, nucleosomes and nucleosomal arrays. These studies highlight the particular strength of NMR in studying nucleosome dynamics and nucleosome-protein interactions. Finally, we look ahead to exciting new possibilities that will be afforded by on-going developments in solution and solid-state NMR. By increasing both the depth and breadth of nucleosome NMR studies, it will be possible to offer a unique perspective on the dynamic landscape of nucleosomes and its interacting proteins.</p></div>","PeriodicalId":20740,"journal":{"name":"Progress in Nuclear Magnetic Resonance Spectroscopy","volume":"110 ","pages":"Pages 1-19"},"PeriodicalIF":6.1,"publicationDate":"2019-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.pnmrs.2019.01.002","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"36998190","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"High-resolution methods for the measurement of scalar coupling constants","authors":"Yanqin Lin ,&nbsp;Qing Zeng ,&nbsp;Liangjie Lin ,&nbsp;Zhong Chen ,&nbsp;Peter B. Barker","doi":"10.1016/j.pnmrs.2018.08.003","DOIUrl":"10.1016/j.pnmrs.2018.08.003","url":null,"abstract":"<div><p>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 <em>J</em> values is often not straightforward because of complex signal splitting patterns and signal overlap. Many methods have been proposed for the measurement of scalar coupling constants, both for homonuclear and heteronuclear cases. Different approaches to the measurement of scalar coupling constants are reviewed here with several applications presented. The accurate measurement of scalar coupling constants can greatly facilitate molecular structure elucidation and the study of molecule dynamics.</p></div>","PeriodicalId":20740,"journal":{"name":"Progress in Nuclear Magnetic Resonance Spectroscopy","volume":"109 ","pages":"Pages 135-159"},"PeriodicalIF":6.1,"publicationDate":"2018-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.pnmrs.2018.08.003","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"36760940","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Structure determination of supra-molecular assemblies by solid-state NMR: Practical considerations","authors":"Jean-Philippe Demers ,&nbsp;Pascal Fricke ,&nbsp;Chaowei Shi ,&nbsp;Veniamin Chevelkov ,&nbsp;Adam Lange","doi":"10.1016/j.pnmrs.2018.06.002","DOIUrl":"10.1016/j.pnmrs.2018.06.002","url":null,"abstract":"<div><p>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.</p><p>This review provides a practical guide for the first steps of studying biological supra-molecular assemblies using ssNMR. The production of isotope-labeled samples is achievable via several means, which include recombinant expression, cell-free protein synthesis, extraction of assemblies directly from cells, or even the study of assemblies in whole cells <em>in situ</em>. Specialized isotope labeling schemes greatly facilitate the assignment of chemical shifts and the collection of structural data. Advanced strategies such as mixed, diluted, or segmental subunit labeling offer the possibility to study inter-molecular interfaces.</p><p>Detailed and practical considerations are presented with respect to first setting up magic-angle spinning (MAS) ssNMR experiments, including the selection of the ssNMR rotor, different methods to best transfer the sample and prepare the rotor, as well as common and robust procedures for the calibration of the instrument. Diagnostic spectra to evaluate the resolution and sensitivity of the sample are presented. Possible improvements that can reduce sample heterogeneity and improve the quality of ssNMR spectra are reviewed.</p></div>","PeriodicalId":20740,"journal":{"name":"Progress in Nuclear Magnetic Resonance Spectroscopy","volume":"109 ","pages":"Pages 51-78"},"PeriodicalIF":6.1,"publicationDate":"2018-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.pnmrs.2018.06.002","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"36760942","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Characterization of intrinsically disordered proteins and their dynamic complexes: From in vitro to cell-like environments","authors":"Sigrid Milles,&nbsp;Nicola Salvi,&nbsp;Martin Blackledge,&nbsp;Malene Ringkjøbing Jensen","doi":"10.1016/j.pnmrs.2018.07.001","DOIUrl":"10.1016/j.pnmrs.2018.07.001","url":null,"abstract":"<div><p>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. We describe the complementarity of different NMR parameters for quantifying the conformational propensities of IDPs in their isolated and phosphorylated states, and we discuss the challenges associated with obtaining structural models of dynamic protein-protein complexes involving IDPs. In addition, we review recent progress in understanding the conformational behavior of IDPs in cell-like environments such as in the presence of crowding agents, in membrane-less organelles and in the complex environment of the human cell.</p></div>","PeriodicalId":20740,"journal":{"name":"Progress in Nuclear Magnetic Resonance Spectroscopy","volume":"109 ","pages":"Pages 79-100"},"PeriodicalIF":6.1,"publicationDate":"2018-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.pnmrs.2018.07.001","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"36760944","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Pros and cons of ultra-high-field MRI/MRS for human application","authors":"Mark E. Ladd ,&nbsp;Peter Bachert ,&nbsp;Martin Meyerspeer ,&nbsp;Ewald Moser ,&nbsp;Armin M. Nagel ,&nbsp;David G. Norris ,&nbsp;Sebastian Schmitter ,&nbsp;Oliver Speck ,&nbsp;Sina Straub ,&nbsp;Moritz Zaiss","doi":"10.1016/j.pnmrs.2018.06.001","DOIUrl":"10.1016/j.pnmrs.2018.06.001","url":null,"abstract":"<div><p>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. On the other side of the scale are gains in signal-to-noise or contrast-to-noise ratio that allow finer structures to be visualized and smaller physiological effects to be detected. This review presents an overview of some of the latest methodological developments in human ultra-high field MRI/MRS as well as associated clinical and scientific applications. Emphasis is given to techniques that particularly benefit from the changing physical characteristics at high magnetic fields, including susceptibility-weighted imaging and phase-contrast techniques, imaging with X-nuclei, MR spectroscopy, CEST imaging, as well as functional MRI. In addition, more general methodological developments such as parallel transmission and motion correction will be discussed that are required to leverage the full potential of higher magnetic fields, and an overview of relevant physiological considerations of human high magnetic field exposure is provided.</p></div>","PeriodicalId":20740,"journal":{"name":"Progress in Nuclear Magnetic Resonance Spectroscopy","volume":"109 ","pages":"Pages 1-50"},"PeriodicalIF":6.1,"publicationDate":"2018-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.pnmrs.2018.06.001","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"36760938","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Recent advances in solid-state nuclear magnetic resonance spectroscopy of exotic nuclei","authors":"César Leroy,&nbsp;David L. Bryce","doi":"10.1016/j.pnmrs.2018.08.002","DOIUrl":"10.1016/j.pnmrs.2018.08.002","url":null,"abstract":"<div><p>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 <em>I</em> &gt; 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. We first discuss some of the recent progress in pulse sequences and hardware development which continues to enable researchers to study new kinds of materials as well as previously unfeasible nuclei. This is followed by a survey of applications to a wide range of exotic nuclei (including e.g., ⁹Be, ²⁵Mg, ³³S, ³⁹K, ⁴³Ca, ^47/49Ti, ⁵³Cr, ⁵⁹Co, ⁶¹Ni, ⁶⁷Zn, ⁷³Ge, ⁷⁵As, ⁸⁷Sr, ¹¹⁵In, ¹¹⁹Sn, ^121/123Sb, ^135/137Ba, ^185/187Re, ²⁰⁹Bi), most of them quadrupolar. The scope of the review is the past ten years, <em>i.e.</em>, 2007–2017.</p></div>","PeriodicalId":20740,"journal":{"name":"Progress in Nuclear Magnetic Resonance Spectroscopy","volume":"109 ","pages":"Pages 160-199"},"PeriodicalIF":6.1,"publicationDate":"2018-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.pnmrs.2018.08.002","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"36760941","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}