Nuclear Magnetic Resonance: Principles and Applications

Description

This lecture covers the principles and applications of Nuclear Magnetic Resonance (NMR), focusing on the elucidation of chemical structures and molecular dynamics. It explains the basics of NMR, including the spin of nuclei, magnetic moments, and the interpretation of NMR spectra. The lecture delves into topics such as chemical shift, peak integration, and peak multiplicity. It also discusses the use of NMR in studying complex molecules like proteins and the determination of protein structures. Additionally, it explores the use of NMR in medical imaging, particularly in Magnetic Resonance Imaging (MRI) for visualizing organs and tissues. The lecture concludes with an overview of NMR spectroscopy in three dimensions and its applications in various fields.

Official source

https://mediaspace.epfl.ch/media/0_oisncap3

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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.

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

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 (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.

Nuclear Overhauser effect

The 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.

Nuclear quadrupole resonance

Nuclear quadrupole resonance spectroscopy or NQR is a chemical analysis technique related to nuclear magnetic resonance (NMR). Unlike NMR, NQR transitions of nuclei can be detected in the absence of a magnetic field, and for this reason NQR spectroscopy is referred to as "zero Field NMR". The NQR resonance is mediated by the interaction of the electric field gradient (EFG) with the quadrupole moment of the nuclear charge distribution.