NMR, a tool for biology.

This review presents the latest update, applications, techniques of the NMR tools in both laboratory and field scales in the oil and gas upstream industry. The applications of NMR in the laboratory scale were thoroughly reviewed and summarized such as porosity, pores size distribution, permeability, saturations, capillary pressure, and wettability. NMR is an emerging tool to evaluate the improved oil recovery techniques, and it was found to be better than the current techniques used for screening, evaluation, and assessment. For example, NMR can define the recovery of oil/gas from the different pore systems in the rocks compared to other macroscopic techniques that only assess the bulk recovery. This manuscript included different applications for the NMR in enhanced oil recovery research. Also, NMR can be used to evaluate the damage potential of drilling, completion, and production fluids laboratory and field scales. Currently, NMR is used to evaluate the emulsion droplet size and its behavior in the pore space in different applications such as enhanced oil recovery, drilling, completion, etc. NMR tools in the laboratory and field scales can be used to assess the unconventional gas resources and NMR showed a very good potential for exploration and production advancement in unconventional gas fields compared to other tools. Field applications of NMR during exploration and drilling such as logging while drilling, geosteering, etc., were reviewed as well. Finally, the future and potential research directions of NMR tools were introduced which include the application of multi-dimensional NMR and the enhancement of the signal-to-noise ratio of the collected data during the logging while drilling operations.

This paper presents a comprehensive review of the recent advances in nuclear magnetic resonance (NMR) measurements for near-surface characterization using laboratory, borehole, and field technologies. During the last decade, NMR has become increasingly popular in near-surface geophysics due to substantial improvements in instrumentation, data processing, forward modeling, inversion, and measurement techniques. This paper starts with a description of the principal theory and applications of NMR. It presents a basic overview of near-surface NMR theory in terms of its physical background and discusses how NMR relaxation times are related to different relaxation processes occurring in porous media. As a next step, the recent and seminal near-surface NMR developments at each scale are discussed, and the limitations and challenges of the measurement are examined. To represent the growth of applications of near-surface NMR, case studies in a variety of different near-surface environments are reviewed and, as examples, two recent case studies are discussed in detail. Finally, this review demonstrates that there is a need for continued research in near-surface NMR and highlights necessary directions for future research. These recommendations include improving the signal-to-noise ratio, reducing the effective measurement dead time, and improving production rate of surface NMR (SNMR), reducing the minimum echo time of borehole NMR (BNMR) measurements, improving petrophysical NMR models of hydraulic conductivity and vadose zone parameters, and understanding the scale dependency of NMR properties.

NMR in Environmental Science

By means of optical pumping with laser light, the nuclear spin polarization of gaseous xenon can be enhanced by many orders of magnitude. The enhanced polarization has allowed an extension of the pioneering experiments of Fraissard and coworkers to novel applications of NMR and MRI in chemistry, materials science and biomedicine. Examples are presented of developments and applications of laser-polarized xenon NMR and MRI on distance scales from nanometers to meters. The size of the xenon atom is similar to that of small organic molecules, such as methane, yet the nuclear magnetic resonance (NMR) signal from xenon proves a more sensitive probe for the local environment. Laser-polarized xenon NMR has been used, in collaboration with Sozzani and coworkers, to investigate the interactions present in an effectively one- dimensional gas phase inside nanochannels. Small changes in channel size and/or structure lead to very different modes of diffusion. Optically pumped Xe NMR can distinguish between these different diffusion modes out to unparalleled time scales (several tens of seconds). These studies are particularly useful for gaining a fundamental understanding of the laws that govern heterogenous mass transport such as gas transport into porous catalysts or molecular sieves, or liquid transport through pore-forming transmembrane proteins in biological systems. The understanding of mass transport inside microporous materials is crucial for many industrial and commercial processes. Recent experiments will also be described in which xenon has been used to investigate the cavities of biological nanosystems and in which polarization has been transferred to molecules on surfaces and in solution. As an example, in collaboration with Wemmer and coworkers, xenon has been used as a molecular probe to investigate the hydrophobic surfaces and interiors of macrocyclic molecules and proteins; recent results show evidence for binding of xenon to the outside of a protein, a proposed cause of the anesthetic mechanism of xenon. Indeed, localized injection of polarized xenon solutions into human blood has provided observations of the real-time process of xenon penetrating red blood cells. The injection technique also makes it possible to provide enhanced magnetic resonance images of localized areas in living organisms. Furthermore, the use of laser-polarized xenon also opens an exciting new frontier in the possibility of “functionalized xenon” as a biosensor of analytes and metabolites in chemistry, materials science and biomedicine. The novel biosensor offers advantages of multiplexing capabilities and the possibility of detection in-vivo.

Applications of nuclear magnetic resonance in lipid analyses: An emerging powerful tool for lipidomics studies

Applications of NMR to Food to Food Science

Understanding the kinetics of proteins interacting with their ligands is important for characterizing molecular mechanism. However, it can be difficult to determine the extent and nature of these interactions for weakly formed protein-ligand complexes that have lifetimes of micro- to milliseconds. Nuclear magnetic resonance (NMR) spectroscopy is a powerful solution-based method for the atomic-level analysis of molecular interactions on a wide range of timescales, including micro- to milliseconds. Recently the combination of thermodynamic experiments using isothermal titration calorimetry (ITC) with kinetic measurements using ZZ-exchange and CPMG relaxation dispersion NMR spectroscopy have been used to determine the kinetics of weakly interacting protein systems. This chapter describes the application of ITC and NMR to understand the differences in the kinetics of carbohydrate binding by the β1- and β2-carbohydrate-binding modules of AMP-activated protein kinase.

BackgroundSoftware for nuclear magnetic resonance (NMR) spectrometers offer general functionality of instrument control and data processing; these applications are often developed with non-scripting languages. NMR users need to flexibly integrate rapidly developing NMR applications with emerging technologies. Scripting systems offer open environments for NMR users to write custom programs. However, existing scripting systems have limited capabilities for both extending the functionality of NMR software’s non-script main program and using advanced native script libraries to support specialized application domains (e.g., biomacromolecules and metabolomics). Therefore, it is essential to design a novel scripting system to address both of these needs.ResultHere, a novel NMR scripting system named SpinSPJ is proposed. It works as a plug-in in the Java based NMR spectrometer software SpinStudioJ. In the scripting system, both Java based NMR methods and original CPython based libraries are supported. A module has been developed as a bridge to integrate the runtime environments of Java and CPython. The module works as an extension in the CPython environment and interacts with Java via the Java Native Interface. Leveraging this bridge, Java based instrument control and data processing methods of SpinStudioJ can be called with the CPython style. Compared with traditional scripting systems, SpinSPJ better supports both extending the non-script main program and implementing advanced NMR applications with a rich variety of script libraries. NMR researchers can easily call functions of instrument control and data processing as well as developing complex functionality (such as multivariate statistical analysis, deep learning, etc.) with CPython native libraries.ConclusionSpinSPJ offers a user-friendly environment to implement custom functionality leveraging its powerful basic NMR and rich CPython libraries. NMR applications with emerging technologies can be easily integrated. The scripting system is free of charge and can be downloaded by visiting http://www.spinstudioj.net/spinspj.

Editorial overview: New protein production tools for structural biology

Paul Christian Lauterbur

NMR Studies of Fossilized Wood

Applications of NMR in heparin and low molecular weight heparins

1. Transverse relaxation and the molecular size limit in liquid state NMR 1612. TROSY: how does it work? 1632.1 Transverse relaxation in coupled spin systems 1632.2 The TROSY effect, relaxation due to remote protons and 2H isotope labeling 1653. Direct heteronuclear chemical shift correlations 1683.1 Single-Quantum [15N,1H]-TROSY 1683.2 Zero-Quantum [15N,1H]-TROSY 1713.3 Single-Quantum TROSY with aromatic 13C–1H moieties 1764. Resonance assignment and NOE spectroscopy of large biomolecules 1804.1 TROSY-based triple resonance experiments for 13C, 15N and 1HN backbone resonance assignment in uniformly 2H, 13C, 15N labeled proteins 1804.2 TROSY-type NOE spectroscopy 1865. Scalar coupling across hydrogen bonds observed by TROSY 1876. The use of TROSY for measurements of residual dipolar coupling constants 1907. Conclusions 1918. Acknowledgements 1919. References 191The application of nuclear magnetic resonance (NMR) spectroscopy for structure determination of proteins and nucleic acids (Wüthrich, 1986) with molecular mass exceeding 30 kDa is largely constrained by two factors, fast transverse relaxation of spins of interest and complexity of NMR spectra, both of which increase with increasing molecular size (Wagner, 1993b; Clore & Gronenborn, 1997, 1998b; Kay & Gardner, 1997). The good news is that neither of these factors represent a fundamental limit for the application of NMR techniques to protein structure determination in solution (Clore & Gronenborn, 1998a; Wüthrich, 1998; Wider & Wüthrich, 1999). In fact, in the past few years the size limitations imposed by these factors have been pushed up to 50–70 kDa by the use of 13C, 15N and 2H isotope labeling combined with selective reprotonation of individual chemical groups in conjunction with the use of triple-resonance experiments (Bax, 1994; Gardner et al. 1997; Gardner & Kay, 1998) and heteronuclear-resolved NMR (Fesik & Zuiderweg, 1988; Marion et al. 1989a; Otting & Wüthrich, 1990). Among the largest biomolecules whose 3D structure was solved by NMR are the 44 kDa trimeric ectodomain of simian immunodeficiency virus (SIV) gp41 (Caffrey et al. 1998) and 40–60 kDa particles of the elongation initiation factor 4E solubilized in CHAPS micelles (Matsuo et al. 1997; McGuire et al. 1998).

Pharmaceutical Applications of NMR

5 - Applications of Nuclear Magnetic Resonance and Mass Spectrometry to Anticancer Drug Discovery