Lecture

Effect of relaxation on magnetization

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Description

This lecture covers the importance of NMR spectroscopy for chemists, focusing on the effect of relaxation on magnetization. It explains the Bloch equations, T1 and T2 effects on the signal, optimal conditions to measure T1 using inversion recovery, and the choice of flip angle for T1 measurement.

In MOOC

Fundamentals of Biomedical Imaging: Magnetic Resonance Imaging (MRI)

This physics course covers the physical principles of major in vivo bio-imaging modalities. This course will focus on magnetic resonance imaging, also known as an MRI. In the first part of the course, the dynamic of spins in a magnetic field is described, leading to the essential notions of magnetic resonance (MR), excitation and relaxation. We will also discuss the basic mechanisms of image reconstruction, MR spectroscopy and functional MRI. You will learn how existing physical principles transcend into bi

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Related concepts (32)

Spin–lattice relaxation

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.

Spin–spin relaxation

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.

Nuclear magnetic resonance spectroscopy

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.

Nuclear magnetic resonance spectroscopy of proteins

Nuclear 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.

Two-dimensional nuclear magnetic resonance spectroscopy

Two-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.

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