NMR-STAR is an extension of the STAR file format to store the results of biological NMR experiments.
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Richard Robert Ernst was a Swiss physical chemist and Nobel Laureate.
The Protein Data Bank (PDB) is a database for the three-dimensional structural data of large biological molecules, such as proteins and nucleic acids. The data, typically obtained by X-ray crystallography, NMR spectroscopy, or, increasingly, cryo-electron microscopy, and submitted by biologists and biochemists from around the world, are freely accessible on the Internet via the websites of its member organisations. The PDB is overseen by an organization called the Worldwide Protein Data Bank, wwPDB.
Kurt Wüthrich is a Swiss chemist/biophysicist and Nobel Chemistry laureate, known for developing nuclear magnetic resonance (NMR) methods for studying biological macromolecules.
In nuclear magnetic resonance (NMR) spectroscopy, the chemical shift is the resonant frequency of an atomic nucleus relative to a standard in a magnetic field. Often the position and number of chemical shifts are diagnostic of the structure of a molecule. Chemical shifts are also used to describe signals in other forms of spectroscopy such as photoemission spectroscopy.
The Nilgiri Mountain Railway (NMR) is a 1,000 mmmetre gauge railway in Tamil Nadu, India, built by the British in 1908. The railway is operated by the Southern Railway and is the only rack railway in India.
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. 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.
Normanton railway station serves the town of Normanton in West Yorkshire, England. It lies 11 miles (18 km) south-east of Leeds railway station on the Hallam Line, which is operated by Northern.
The Queen Nandi Mounted Rifles is an reserve armoured regiment of the South African Army.
Carbon-13 (C13) nuclear magnetic resonance is the application of nuclear magnetic resonance (NMR) spectroscopy to carbon. It is analogous to proton NMR and allows the identification of carbon atoms in an organic molecule just as proton NMR identifies hydrogen atoms. 13C NMR detects only the 13
C
isotope. The main carbon isotope, 12
C
is not detected. Although much less sensitive than 1H NMR spectroscopy, 13C NMR spectroscopy is widely used for characterizing organic and organometallic compounds.
Proton nuclear magnetic resonance is the application of nuclear magnetic resonance in NMR spectroscopy with respect to hydrogen-1 nuclei within the molecules of a substance, in order to determine the structure of its molecules. In samples where natural hydrogen (H) is used, practically all the hydrogen consists of the isotope 1H.
Nuclear magnetic resonance spectroscopy of proteins is a field of structural biology in which NMR spectroscopy is used to obtain information about the structure and dynamics of proteins, and also nucleic acids, and their complexes. The field was pioneered by Richard R. Ernst and Kurt Wüthrich at the ETH, and by Ad Bax, Marius Clore, Angela Gronenborn at the NIH, and Gerhard Wagner at Harvard University, among others. Structure determination by NMR spectroscopy usually consists of several phases, each using a separate set of highly specialized techniques. The sample is prepared, measurements are made, interpretive approaches are applied, and a structure is calculated and validated.
Two-dimensional nuclear magnetic resonance spectroscopy is a set of nuclear magnetic resonance spectroscopy (NMR) methods which give data plotted in a space defined by two frequency axes rather than one. Types of 2D NMR include correlation spectroscopy (COSY), J-spectroscopy, exchange spectroscopy (EXSY), and nuclear Overhauser effect spectroscopy (NOESY). Two-dimensional NMR spectra provide more information about a molecule than one-dimensional NMR spectra and are especially useful in determining the structure of a molecule, particularly for molecules that are too complicated to work with using one-dimensional NMR.
Alexander Pines is an American chemist. He is the Glenn T. Seaborg Professor Emeritus, University of California, Berkeley, Chancellor's Professor Emeritus and Professor of the Graduate School, University of California, Berkeley, and a member of the California Institute for Quantitative Biosciences (QB3) and the Department of Bioengineering. He was born in 1945, grew up in Bulawayo in Southern Rhodesia and studied undergraduate mathematics and chemistry in Israel at Hebrew University of Jerusalem. Coming to the United States in 1968, Pines obtained his Ph.D. in chemical physics at M.I.T. in 1972 and joined the UC Berkeley faculty later that year.
Nuclear magnetic resonance quantum computing (NMRQC) is one of the several proposed approaches for constructing a quantum computer, that uses the spin states of nuclei within molecules as qubits. The quantum states are probed through the nuclear magnetic resonances, allowing the system to be implemented as a variation of nuclear magnetic resonance spectroscopy. NMR differs from other implementations of quantum computers in that it uses an ensemble of systems, in this case molecules, rather than a single pure state.
An NMR tube is a thin glass walled tube used to contain samples in nuclear magnetic resonance spectroscopy. Typically NMR tubes come in 5 mm diameters but 10 mm and 3 mm samples are known. It is important that the tubes are uniformly thick and well-balanced to ensure that NMR tube spins at a regular rate, usually about 20 Hz in the NMR spectrometer.
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.
Robert Vivian Pound was a Canadian-American physicist who helped discover nuclear magnetic resonance (NMR) and who devised the famous Pound–Rebka experiment supporting general relativity. He became a tenured professor of physics at Harvard without ever having received a graduate degree.
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).
The Biological Magnetic Resonance Data Bank is an open access repository of nuclear magnetic resonance (NMR) spectroscopic data from peptides, proteins, nucleic acids and other biologically relevant molecules. The database is operated by the University of Wisconsin–Madison and is supported by the National Library of Medicine. The BMRB is part of the Research Collaboratory for Structural Bioinformatics and, since 2006, it is a partner in the Worldwide Protein Data Bank (wwPDB). The repository accepts NMR spectral data from laboratories around the world and, once the data is validated, it is available online at the BMRB website. The database has also an ftp site, where data can be downloaded in the bulk. The BMRB has two mirror sites, one at the Protein Database Japan (PDBj) at Osaka University and one at the Magnetic Resonance Research Center (CERM) at the University of Florence in Italy. The site at Japan accepts and processes data depositions.