Spin diffusion

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Spin diffusion describes a situation wherein the individual nuclear spins undergo continuous exchange of energy. [1] This permits polarization differences within the sample to be reduced on a timescale much shorter than relaxation effects. [1]

Spin diffusion is a process by which magnetization can be exchanged spontaneously between spins. The process is driven by dipolar coupling, and is therefore related to internuclear distances. Spin diffusion has been used to study many structural problems in the past, ranging from domain sizes in polymers and disorder in glassy materials to high-resolution crystal structure determination of small molecules and proteins.

In solid-state nuclear magnetic resonance, spin diffusion plays a major role in Cross Polarization (CP) experiments. As mentioned before, by transferring the magnetization (and thus the population) from nuclei with different values for the spin-lattice relaxation (T1), the overall time for the experiment is reduced. Is a very common practice when the sample contains hydrogen. Another desirable effect is that the signal to noise ratio (S/N) is increased until a theoretical factor γAB, being γ the gyromagnetic ratio.

Notes

  1. 1 2 EPS2:Spin-Diffusion


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<span class="mw-page-title-main">Nuclear magnetic resonance spectroscopy</span> Laboratory technique

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.

<span class="mw-page-title-main">Solid-state nuclear magnetic resonance</span>

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.

<span class="mw-page-title-main">Muon spin spectroscopy</span>

Muon spin spectroscopy, also known as µSR, is an experimental technique based on the implantation of spin-polarized muons in matter and on the detection of the influence of the atomic, molecular or crystalline surroundings on their spin motion. The motion of the muon spin is due to the magnetic field experienced by the particle and may provide information on its local environment in a very similar way to other magnetic resonance techniques, such as electron spin resonance and, more closely, nuclear magnetic resonance (NMR).

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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.

In MRI and NMR spectroscopy, an observable nuclear spin polarization (magnetization) is created by a homogeneous magnetic field. This field makes the magnetic dipole moments of the sample precess at the resonance (Larmor) frequency of the nuclei. At thermal equilibrium, nuclear spins precess randomly about the direction of the applied field. They become abruptly phase coherent when they are hit by radiofrequency (RF) pulses at the resonant frequency, created orthogonal to the field. The RF pulses cause the population of spin-states to be perturbed from their thermal equilibrium value. The generated transverse magnetization can then induce a signal in an RF coil that can be detected and amplified by an RF receiver. The return of the longitudinal component of the magnetization to its equilibrium value is termed spin-latticerelaxation while the loss of phase-coherence of the spins is termed spin-spin relaxation, which is manifest as an observed free induction decay (FID).

Insensitive nuclei enhancement by polarization transfer (INEPT) is a signal enhancement method used in NMR spectroscopy. It involves the transfer of nuclear spin polarization from spins with large Boltzmann population differences to nuclear spins of interest with lower Boltzmann population differences. INEPT uses J-coupling for the polarization transfer in contrast to Nuclear Overhauser effect (NOE), which arises from dipolar cross-relaxation. This method of signal enhancement was introduced by Ray Freeman in 1979. Due to its usefulness in signal enhancement, pulse sequences used in heteronuclear NMR experiments often contain blocks of INEPT or INEPT-like sequences.

A spin exchange relaxation-free (SERF) magnetometer is a type of magnetometer developed at Princeton University in the early 2000s. SERF magnetometers measure magnetic fields by using lasers to detect the interaction between alkali metal atoms in a vapor and the magnetic field.

<span class="mw-page-title-main">Spin–spin relaxation</span>

In 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. It is the time it takes for the magnetic resonance signal to irreversibly decay to 37% (1/e) of its initial value after its generation by tipping the longitudinal magnetization towards the magnetic transverse plane. Hence the relation

During 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.

<span class="mw-page-title-main">Zero field NMR</span> Acquisition of NMR spectra of chemicals

Zero- to ultralow-field (ZULF) NMR is the acquisition of nuclear magnetic resonance (NMR) spectra of chemicals with magnetically active nuclei in an environment carefully screened from magnetic fields. ZULF NMR experiments typically involve the use of passive or active shielding to attenuate Earth’s magnetic field. This is in contrast to the majority of NMR experiments which are performed in high magnetic fields provided by superconducting magnets. In ZULF experiments the dominant interactions are nuclear spin-spin couplings, and the coupling between spins and the external magnetic field is a perturbation to this. There are a number of advantages to operating in this regime: magnetic-susceptibility-induced line broadening is attenuated which reduces inhomogeneous broadening of the spectral lines for samples in heterogeneous environments. Another advantage is that the low frequency signals readily pass through conductive materials such as metals due to the increased skin depth; this is not the case for high-field NMR for which the sample containers are usually made of glass, quartz or ceramic.

Magnetization transfer (MT), in NMR and MRI, refers to the transfer of nuclear spin polarization and/or spin coherence from one population of nuclei to another population of nuclei, and to techniques that make use of these phenomena. There is some ambiguity regarding the precise definition of magnetization transfer, however the general definition given above encompasses all more specific notions. NMR active nuclei, those with non-zero spin, can be energetically coupled to one another under certain conditions. The mechanisms of nuclear-spin energy-coupling have been extensively characterized and are described in the following articles: Angular momentum coupling, Magnetic dipole–dipole interaction, J-coupling, Residual dipolar coupling, Nuclear Overhauser effect, Spin–spin relaxation, and Spin saturation transfer. Alternatively, some nuclei in a chemical system are labile and exchange between non-equivalent environments. A more specific example of this case is presented in the section Chemical Exchange Magnetization transfer.

Nuclear magnetic resonance (NMR) in porous materials covers the application of using NMR as a tool to study the structure of porous media and various processes occurring in them. This technique allows the determination of characteristics such as the porosity and pore size distribution, the permeability, the water saturation, the wettability, etc.

<span class="mw-page-title-main">Nuclear magnetic resonance</span> Spectroscopic technique based on change of nuclear spin state

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<span class="mw-page-title-main">Pulsed electron paramagnetic resonance</span>

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<span class="mw-page-title-main">Cross-polarization</span> Spectroscopy technique

Cross-polarization (CP), originally published as proton-enhanced nuclear induction spectroscopy is a solid-state nuclear magnetic resonance (ssNMR) technique to transfer nuclear magnetization from different types of nuclei via heteronuclear dipolar interactions. The 1H-X cross-polarization dramatically improves the sensitivity of ssNMR experiments of most experiments involving spin-1/2 nuclei, capitalizing on the higher 1H polarisation, and shorter T1(1H) relaxation times. It was developed by Michael Gibby, Alexander Pines and Professor John S. Waugh at the Massachusetts Institute of Technology.