Nuclear magnetic resonance spectroscopy, most commonly known as NMR spectroscopy or magnetic resonance spectroscopy (MRS), is a spectroscopic technique to observe local magnetic fields around atomic nuclei. This spectroscopy is based on the measurement of absorption of electromagnetic radiations in the radio frequency region from roughly 4 to 900 MHz. Absorption of radio waves in the presence of magnetic field is accompanied by a special type of nuclear transition, and for this reason, such type of spectroscopy is known as Nuclear Magnetic Resonance Spectroscopy. The sample is placed in a magnetic field and the NMR signal is produced by excitation of the nuclei sample with radio waves into nuclear magnetic resonance, which is detected with sensitive radio receivers. The intramolecular magnetic field around an atom in a molecule changes the resonance frequency, thus giving access to details of the electronic structure of a molecule and its individual functional groups. As the fields are unique or highly characteristic to individual compounds, in modern organic chemistry practice, NMR spectroscopy is the definitive method to identify monomolecular organic compounds.
Solid-state NMR (ssNMR) spectroscopy is a technique for characterizing atomic level structure in solid materials e.g. powders, single crystals and amorphous samples and tissues using nuclear magnetic resonance (NMR) spectroscopy. The anisotropic part of many spin interactions are present in solid-state NMR, unlike in solution-state NMR where rapid tumbling motion averages out many of the spin interactions. As a result, solid-state NMR spectra are characterised by larger linewidths than in solution state NMR, which can be utilized to give quantitative information on the molecular structure, conformation and dynamics of the material. Solid-state NMR is often combined with magic angle spinning to remove anisotropic interactions and improve the resolution as well as the sensitivity of the technique.
The Journal of Biomolecular NMR publishes research on technical developments and innovative applications of nuclear magnetic resonance spectroscopy for the study of structure and dynamic properties of biopolymers in solution, liquid crystals, solids and mixed environments. Some of the main topics include experimental and computational approaches for the determination of three-dimensional structures of proteins and nucleic acids, advancements in the automated analysis of NMR spectra, and new methods to probe and interpret molecular motions.
Herbert Sander Gutowsky was an American chemist who was a Professor of Chemistry at the University of Illinois Urbana-Champaign. Gutowsky was the first to apply nuclear magnetic resonance (NMR) methods to the field of chemistry. He used nuclear magnetic resonance spectroscopy to determine the structure of molecules. His pioneering work developed experimental control of NMR as a scientific instrument, connected experimental observations with theoretical models, and made NMR one of the most effective analytical tools for analysis of molecular structure and dynamics in liquids, solids, and gases, used in chemical and medical research, His work was relevant to the solving of problems in chemistry, biochemistry, and materials science, and has influenced many of the subfields of more recent NMR spectroscopy.
Charles Pence Slichter was an American physicist, best known for his work on nuclear magnetic resonance and superconductivity.
Nuclear magnetic resonance (NMR) is a physical phenomenon in which nuclei in a strong constant magnetic field are perturbed by a weak oscillating magnetic field and respond by producing an electromagnetic signal with a frequency characteristic of the magnetic field at the nucleus. This process occurs near resonance, when the oscillation frequency matches the intrinsic frequency of the nuclei, which depends on the strength of the static magnetic field, the chemical environment, and the magnetic properties of the isotope involved; in practical applications with static magnetic fields up to ca. 20 tesla, the frequency is similar to VHF and UHF television broadcasts (60–1000 MHz). NMR results from specific magnetic properties of certain atomic nuclei. Nuclear magnetic resonance spectroscopy is widely used to determine the structure of organic molecules in solution and study molecular physics and crystals as well as non-crystalline materials. NMR is also routinely used in advanced medical imaging techniques, such as in magnetic resonance imaging (MRI).
Antony John Williams is a British chemist and expert in the fields of both nuclear magnetic resonance (NMR) spectroscopy and cheminformatics at the United States Environmental Protection Agency. He is the founder of the ChemSpider website that was purchased by the Royal Society of Chemistry in May 2009. He is a science blogger and an author.
Nucleic acid NMR is the use of nuclear magnetic resonance spectroscopy to obtain information about the structure and dynamics of nucleic acid molecules, such as DNA or RNA. It is useful for molecules of up to 100 nucleotides, and as of 2003, nearly half of all known RNA structures had been determined by NMR spectroscopy.
Computer-assisted structure elucidation is the technique of using software to generate all possible molecular structures that are consistent with a particular set of spectroscopic data. The subject has been often reviewed. Available CASE software include LSD, SENECA, COCON, CMC-se, and Structure Elucidator.
The chemical shift index or CSI is a widely employed technique in protein nuclear magnetic resonance spectroscopy that can be used to display and identify the location as well as the type of protein secondary structure found in proteins using only backbone chemical shift data The technique was invented by David S. Wishart in 1992 for analyzing 1Hα chemical shifts and then later extended by him in 1994 to incorporate 13C backbone shifts. The original CSI method makes use of the fact that 1Hα chemical shifts of amino acid residues in helices tends to be shifted upfield relative to their random coil values and downfield in beta strands. Similar kinds of upfield and downfield trends are also detectable in backbone 13C chemical shifts.
Gareth Alun Morris FRS is a Professor of Physical Chemistry, in the School of Chemistry at the University of Manchester.
G. Marius Clore MAE, FRSC, FRS is a British-born, Anglo-American molecular biophysicist and structural biologist. He was born in London, U.K. and is a dual U.S./U.K. Citizen. He is a Member of the National Academy of Sciences, a Fellow of the Royal Society, a NIH Distinguished Investigator, and the Chief of the Molecular and Structural Biophysics Section in the Laboratory of Chemical Physics of the National Institute of Diabetes and Digestive and Kidney Diseases at the U.S. National Institutes of Health. He is known for his foundational work in three-dimensional protein and nucleic acid structure determination by biomolecular NMR spectroscopy, for advancing experimental approaches to the study of large macromolecules and their complexes by NMR, and for developing NMR-based methods to study rare conformational states in protein-nucleic acid and protein-protein recognition. Clore's discovery of previously undetectable, functionally significant, rare transient states of macromolecules has yielded fundamental new insights into the mechanisms of important biological processes, and in particular the significance of weak interactions and the mechanisms whereby the opposing constraints of speed and specificity are optimized. Further, Clore's work opens up a new era of pharmacology and drug design as it is now possible to target structures and conformations that have been heretofore unseen.
David Lyndon Emsley FRSC is a British chemist specialising in solid-state nuclear magnetic resonance and a professor at EPFL. He was awarded the 2012 Grand Prix Charles-Leopold Mayer of the French Académie des Sciences and the 2015 Bourke Award of the Royal Society of Chemistry.
Marc Baldus is a physicist and professor of NMR spectroscopy at Utrecht University. He is especially known for his work in the field of structural biology using solid-state nuclear magnetic resonance (ssNMR) spectroscopy. He applies ssNMR methods to establish structure-function relationships in complex biomolecular systems including membrane and Amyloid proteins. In addition, he develops cellular NMR methods to study large molecular transport and insertion systems in bacteria as well as signal transduction mechanisms in eukaryotic cells.
Svyatoslav Petrovich Gabuda was a Soviet/Russian physicist, professor, and doctor of physical and mathematical sciences.
Lucio Frydman is an Israeli chemist whose research focuses on magnetic resonance imaging (MRI), nuclear magnetic resonance (NMR) and solid-state NMR. He was awarded the 2000 Günther Laukien Prize, the 2013 Russell Varian Prize and the 2021 Ernst Prize. He is Professor and Head of the Department of Chemical and Biological Physics at the Weizmann Institute of Science in Israel and Chief Scientist in Chemistry and Biology at the US National High Magnetic Field Laboratory in Tallahassee, Florida. He is a fellow of the International Society of Magnetic Resonance and of the International Society of Magnetic Resonance in Medicine. He was the Editor-in-Chief of the Journal of Magnetic Resonance (2011-2021).
Malcolm Harris Levitt is a British physical chemist and nuclear magnetic resonance (NMR) spectroscopist. He is Professor in Physical Chemistry at the University of Southampton and was elected a Fellow of the Royal Society in 2007.
Mei Hong is a Chinese-American biophysical chemist and Professor of Chemistry at the Massachusetts Institute of Technology. She is known for her creative development and application of solid-state nuclear magnetic resonance (ssNMR) spectroscopy to elucidate the structures and mechanisms of membrane proteins, plant cell walls, and amyloid proteins. She has received a number of recognitions for her work, including the American Chemical Society Nakanishi Prize in 2021, Günther Laukien Prize in 2014, the Protein Society Young Investigator award in 2012, and the American Chemical Society’s Pure Chemistry award in 2003.
Melinda Jane Duer is Professor of Biological and Biomedical Chemistry in the Department of Chemistry at the University of Cambridge, and was the first woman to be appointed to an academic position in the department. Her research investigates changes in molecular structure of the extracellular matrix in tissues in disease and during ageing. She serves as Deputy Warden of Robinson College, Cambridge. She is an editorial board member of the Journal of Magnetic Resonance.
Eric Oldfield is a British chemist, the Harriet A. Harlin Professor of Chemistry and a Professor of Biophysics at the University of Illinois at Urbana-Champaign. He is known for his work in nuclear magnetic resonance spectroscopy of lipids, proteins, and membranes; of inorganic solids; in computational chemistry, and in microbiology and parasitology. He is a member of the American Association for the Advancement of Science, a Fellow of the Royal Society of Chemistry, and a Fellow of the American Physical Society.
