Lecture

Nuclear Magnetic Resonance: Principles and Applications

Graph Chat

Chat with Graph Search

Ask any question about EPFL courses, lectures, exercises, research, news, etc. or try the example questions below.

DISCLAIMER: The Graph Chatbot is not programmed to provide explicit or categorical answers to your questions. Rather, it transforms your questions into API requests that are distributed across the various IT services officially administered by EPFL. Its purpose is solely to collect and recommend relevant references to content that you can explore to help you answer your questions.

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

Ontological neighbourhood

Chemistry

Physical chemistry: Spectroscopy

Related concepts (25)

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.

Magnetic resonance imaging

Magnetic resonance imaging (MRI) is a medical imaging technique used in radiology to form pictures of the anatomy and the physiological processes of the body. MRI scanners use strong magnetic fields, magnetic field gradients, and radio waves to generate images of the organs in the body. MRI does not involve X-rays or the use of ionizing radiation, which distinguishes it from computed tomography (CT) and positron emission tomography (PET) scans.

Related lectures (64)

Relaxation & Structure

Explores relaxation and structure determination in NMR spectroscopy, covering nuclear spin relaxation, anisotropic interactions, NOESY experiments, and protein structure determination protocol.

Protein Structure Determination

Explores protein structure determination using NMR and Cryo-EM techniques, covering chemical shifts, isotope labeling, NOE, and high-resolution imaging methods.

Protein Structure Determination: NMR Insights

Explores NMR spectroscopy for protein structure determination and introduces Cryo-EM as a complementary technique with recent advancements.

Protein Structure Determination: X-ray vs NMR

Explores protein structure determination using X-ray crystallography and NMR spectroscopy, covering historical significance, crystal formation, diffraction patterns, and challenges in crystallization.

Spin Relaxation: Examples and Mechanisms