Nuclear Overhauser effectThe nuclear Overhauser effect (NOE) is the transfer of nuclear spin polarization from one population of spin-active nuclei (e.g. 1H, 13C, 15N etc.) to another via cross-relaxation. A phenomenological definition of the NOE in nuclear magnetic resonance spectroscopy (NMR) is the change in the integrated intensity (positive or negative) of one NMR resonance that occurs when another is saturated by irradiation with an RF field. The change in resonance intensity of a nucleus is a consequence of the nucleus being close in space to those directly affected by the RF perturbation.
Two-dimensional nuclear magnetic resonance spectroscopyTwo-dimensional nuclear magnetic resonance spectroscopy (2D NMR) 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.
Nuclear magnetic resonance spectroscopyNuclear 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.
Nuclear magnetic resonance spectroscopy of proteinsNuclear magnetic resonance spectroscopy of proteins (usually abbreviated protein NMR) 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.
Nuclear magnetic resonanceNuclear magnetic resonance (NMR) is a physical phenomenon in which nuclei in a strong constant magnetic field are perturbed by a weak oscillating magnetic field (in the near 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.
J-couplingIn nuclear chemistry and nuclear physics, J-couplings (also called spin-spin coupling or indirect dipole–dipole coupling) are mediated through chemical bonds connecting two spins. It is an indirect interaction between two nuclear spins that arises from hyperfine interactions between the nuclei and local electrons. In NMR spectroscopy, J-coupling contains information about relative bond distances and angles. Most importantly, J-coupling provides information on the connectivity of chemical bonds.
Solid-state nuclear magnetic resonanceSolid-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.
Spin–lattice relaxationDuring nuclear magnetic resonance observations, spin–lattice relaxation is the mechanism by which the longitudinal component of the total nuclear magnetic moment vector (parallel to the constant magnetic field) exponentially relaxes from a higher energy, non-equilibrium state to thermodynamic equilibrium with its surroundings (the "lattice"). It is characterized by the spin–lattice relaxation time, a time constant known as T1.
Spin echoIn magnetic resonance, a spin echo or Hahn echo is the refocusing of spin magnetisation by a pulse of resonant electromagnetic radiation. Modern nuclear magnetic resonance (NMR) and magnetic resonance imaging (MRI) make use of this effect. The NMR signal observed following an initial excitation pulse decays with time due to both spin relaxation and any inhomogeneous effects which cause spins in the sample to precess at different rates. The first of these, relaxation, leads to an irreversible loss of magnetisation.
Spin–spin relaxationIn physics, the spin–spin relaxation is the mechanism by which Mxy, the transverse component of the magnetization vector, exponentially decays towards its equilibrium value in nuclear magnetic resonance (NMR) and magnetic resonance imaging (MRI). It is characterized by the spin–spin relaxation time, known as T2, a time constant characterizing the signal decay. It is named in contrast to T1, the spin–lattice relaxation time.
Molecular diffusionMolecular diffusion, often simply called diffusion, is the thermal motion of all (liquid or gas) particles at temperatures above absolute zero. The rate of this movement is a function of temperature, viscosity of the fluid and the size (mass) of the particles. Diffusion explains the net flux of molecules from a region of higher concentration to one of lower concentration. Once the concentrations are equal the molecules continue to move, but since there is no concentration gradient the process of molecular diffusion has ceased and is instead governed by the process of self-diffusion, originating from the random motion of the molecules.
DiffusionDiffusion is the net movement of anything (for example, atoms, ions, molecules, energy) generally from a region of higher concentration to a region of lower concentration. Diffusion is driven by a gradient in Gibbs free energy or chemical potential. It is possible to diffuse "uphill" from a region of lower concentration to a region of higher concentration, like in spinodal decomposition. Diffusion is a stochastic process due to the inherent randomness of the diffusing entity and can be used to model many real-life stochastic scenarios.
Protein foldingProtein folding is the physical process where a protein chain is translated into its native three-dimensional structure, typically a "folded" conformation, by which the protein becomes biologically functional. Via an expeditious and reproducible process, a polypeptide folds into its characteristic three-dimensional structure from a random coil. Each protein exists first as an unfolded polypeptide or random coil after being translated from a sequence of mRNA into a linear chain of amino acids.
Carbon-burning processThe carbon-burning process or carbon fusion is a set of nuclear fusion reactions that take place in the cores of massive stars (at least 8 at birth) that combines carbon into other elements. It requires high temperatures (> 5×108 K or 50 keV) and densities (> 3×109 kg/m3). These figures for temperature and density are only a guide. More massive stars burn their nuclear fuel more quickly, since they have to offset greater gravitational forces to stay in (approximate) hydrostatic equilibrium.
CNO cycleThe CNO cycle (for carbon–nitrogen–oxygen; sometimes called Bethe–Weizsäcker cycle after Hans Albrecht Bethe and Carl Friedrich von Weizsäcker) is one of the two known sets of fusion reactions by which stars convert hydrogen to helium, the other being the proton–proton chain reaction (p–p cycle), which is more efficient at the Sun's core temperature. The CNO cycle is hypothesized to be dominant in stars that are more than 1.3 times as massive as the Sun.
AmideIn organic chemistry, an amide, also known as an organic amide or a carboxamide, is a compound with the general formula , where R, R', and R′′ represent any group, typically organyl groups or hydrogen atoms. The amide group is called a peptide bond when it is part of the main chain of a protein, and an isopeptide bond when it occurs in a side chain, such as in the amino acids asparagine and glutamine. It can be viewed as a derivative of a carboxylic acid () with the hydroxyl group () replaced by an amine group (); or, equivalently, an acyl (alkanoyl) group () joined to an amine group.
CarbonCarbon () is a chemical element with the symbol C and atomic number 6. It is nonmetallic and tetravalent—its atom making four electrons available to form covalent chemical bonds. It belongs to group 14 of the periodic table. Carbon makes up about 0.025 percent of Earth's crust. Three isotopes occur naturally, ^12C and ^13C being stable, while ^14C is a radionuclide, decaying with a half-life of about 5,730 years. Carbon is one of the few elements known since antiquity.
Schmidt reactionIn organic chemistry, the Schmidt reaction is an organic reaction in which an azide reacts with a carbonyl derivative, usually an aldehyde, ketone, or carboxylic acid, under acidic conditions to give an amine or amide, with expulsion of nitrogen. It is named after Karl Friedrich Schmidt (1887–1971), who first reported it in 1924 by successfully converting benzophenone and hydrazoic acid to benzanilide. The intramolecular reaction was not reported until 1991 but has become important in the synthesis of natural products.
Heat shock proteinHeat shock proteins (HSP) are a family of proteins produced by cells in response to exposure to stressful conditions. They were first described in relation to heat shock, but are now known to also be expressed during other stresses including exposure to cold, UV light and during wound healing or tissue remodeling. Many members of this group perform chaperone functions by stabilizing new proteins to ensure correct folding or by helping to refold proteins that were damaged by the cell stress.
Carbon cycleThe carbon cycle is that part of the biogeochemical cycle by which carbon is exchanged among the biosphere, pedosphere, geosphere, hydrosphere, and atmosphere of Earth. Other major biogeochemical cycles include the nitrogen cycle and the water cycle. Carbon is the main component of biological compounds as well as a major component of many minerals such as limestone. The carbon cycle comprises a sequence of events that are key to making Earth capable of sustaining life.
