Publication

Utilization of NMR spectroscopy to study biological fluids and metabolic processes: Two introductory activities

Luciano Andres Abriata
2012
Journal Articles

Abstract

This work describes two activities designed to introduce students into the use of NMR spectroscopy for the analysis of biological fluids. In the first activity, 1H spectra of common beverages are acquired and analyzed to identify their most abundant constituents based on computer-aided comparison against known spectra of metabolites. In the second activity, the utilization of glucose by yeast is followed by collecting 1H spectra over time, and the evolution of substrates and products is analyzed. The possibility of tailoring these activities to different levels and course scopes is discussed, together with potential alternative experiments and analyses. (c) 2012 Wiley Periodicals, Inc. Concepts Magn Reson Part A 40A: 171178, 2012.

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https://infoscience.epfl.ch/entities/publication/e68194f3-7294-4a55-b4b5-2a053608f011

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Luciano Andres Abriata
2012
Journal Articles

Abstract

Official source

https://infoscience.epfl.ch/entities/publication/e68194f3-7294-4a55-b4b5-2a053608f011

About this result

Related concepts (20)

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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