This article follows the historical summary and serves as a bridge to five additional overviews of historical developments in NMR during the last two decades. What now seem to be very distinct applications of NMR in biology, medicine, materials science, crystallography, plant sciences, and many other areas trace their origins to the NMR roots in physics, chemistry, and instrumentation. To illustrate the broad scope of current activity, a summary is given of a number of major continuing MR conferences in disparate areas ranging from fundamental MR physics and methodology to clinical medicine, microscopy, and food science.

The phenomenon of hydrogen bonding (H-bonding) has been recognized for almost a century in chemistry and biochemistry to explain weak, directional, attractive forces between electronegative atoms or groups mediated by a hydrogen atom. A variety of physical methods, including NMR, have provided insights into this phenomenon. This article reviews some of the salient features of the H-bond and shows how H-bonding influences principal NMR observables, such as chemical shifts, relaxation times, scalar and quadrupolar coupling constants, as well as hydrogen exchange rates and fractionation factors. We also provide a number of examples that illustrate the use of these NMR parameters for the analysis of the physicochemical nature of the H-bond and of molecular structures, and various processes of physical, chemical, and biological interest.

IUPAC has published a number of recommendations regarding the reporting of nuclear magnetic resonance (NMR) data, especially chemical shifts. The most recent publication [Pure Appl. Chem. 73, 1795 (2001)] recommended that tetramethylsilane (TMS) serve as a universal reference for reporting the shifts of all nuclides, but it deferred recommendations for several aspects of this subject. This document first examines the extent to which the (1)H shielding in TMS itself is subject to change by variation in temperature, concentration, and solvent. On the basis of recently published results, it has been established that the shielding of TMS in solution [along with that of sodium-3-(trimethylsilyl)propanesulfonate, DSS, often used as a reference for aqueous solutions] varies only slightly with temperature but is subject to solvent perturbations of a few tenths of a part per million (ppm). Recommendations are given for reporting chemical shifts under most routine experimental conditions and for quantifying effects of temperature and solvent variation, including the use of magnetic susceptibility corrections and of magic-angle spinning (MAS).This document provides the first IUPAC recommendations for referencing and reporting chemical shifts in solids, based on high-resolution MAS studies. Procedures are given for relating (13)C NMR chemical shifts in solids to the scales used for high-resolution studies in the liquid phase. The notation and terminology used for describing chemical shift and shielding tensors in solids are reviewed in some detail, and recommendations are given for best practice. (C) 2008 IUPAC. Published by Elsevier Inc. All rights reserved.

IUPAC has published a number of recommendations regarding the reporting of nuclear magnetic resonance (NMR) data, especially chemical shifts. The most recent publication [Pure Appl. Chem. 73, 1795 (2001)] recommended that tetramethylsilane (TMS) serve as a universal reference for reporting the shifts of all nuclides, but it deferred recommendations for several aspects of this subject. This document first examines the extent to which the 1H shielding in TMS itself is subject to change by variation in temperature, concentration, and solvent. On the basis of recently published results, it has been established that the shielding of TMS in solution [along with that of sodium-3-(trimethylsilyl)propanesulfonate, DSS, often used as a reference for aqueous solutions] varies only slightly with temperature but is subject to solvent perturbations of a few tenths of a part per million (ppm). Recommendations are given for reporting chemical shifts under most routine experimental conditions and for quantifying effects of temperature and solvent variation, including the use of magnetic susceptibility corrections and of magic-angle spinning (MAS). This document provides the first IUPAC recommendations for referencing and reporting chemical shifts in solids, based on high-resolution MAS studies. Procedures are given for relating 13C NMR chemical shifts in solids to the scales used for high-resolution studies in the liquid phase. The notation and terminology used for describing chemical shift and shielding tensors in solids are reviewed in some detail, and recommendations are given for best practice.

The sections in this article are 1 The Origins of NMR 2 NMR in Bulk Materials 3 NMR —A Tool for Chemical Studies 4 Further Developments in the Physics of NMR 5 NMR in Chemistry Comes of Age 6 Major Advances in NMR Technology 7 Fourier Transform NMR 8 High-Resolution NMR in Solids 9 Multinuclear Magnetic Resonance 10 Biochemical Applications of NMR 11 Two-Dimensional NMR 12 The Evolution of In Vivo NMR 13 Images by NMR 14 Protein Structures by NMR 15 NMR in Materials Science 16 Modern Biomedical Applications of NMR 17 Other Applications of NMR 18 Retrospective and Prospective 19 Acknowledgements 20 Biographical Sketches

The sections in this article are 1 My First Inklings of NMR 2 On to NIH 3 Liddel and Ramsey 4 Early NMR Studies 5 Higher Fields and Larger Molecules 6 Farrar and Becker 7 Further Evolution of NMR at NIH 8 A Final Note 9 Biographical Sketch

The sections in this article are 1 Introduction 2 Nature of the Hydrogen Bond 3 Effect of Hydrogen Bonding on 1 H Chemical Shifts 4 Chemical Shifts of Other Nuclei 5 Scalar Coupling 6 Relaxation Effects 7 Isotope Effects Resulting from Hydrogen Bonds 8 Magnetic Dipole and Electric Quadrupole Interactions in Solids 9 Biographical Sketch Related Articles