Publication

Excitation of Selected Proton Signals in NMR of Isotopically Labeled Macromolecules

Geoffrey Bodenhausen
1999
Journal Articles

Abstract

In isotopically labeled macromols., it is possible to excite the signal of a selected proton by shuttling magnetization back and forth between the chosen proton and a heteronucleus such as 13C or 15N, using two-way doubly selective heteronuclear cross-polarization. Selective excitation of a chosen proton can be followed by homonuclear coherence transfer to identify side-chain resonances of the corresponding amino acid in proteins. The resulting one-dimensional expts. yield information that can usually only be obtained from three-dimensional HSQC-TOCSY spectra. The method also provides efficient suppression of solvent signals without affecting resonances close to the solvent peak. (c) 1999 Academic Press. [on SciFinder (R)]

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https://infoscience.epfl.ch/entities/publication/dd2b5f09-92f4-4711-8e96-1222e030b33f

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Geoffrey Bodenhausen
1999
Journal Articles

Abstract

Official source

https://infoscience.epfl.ch/entities/publication/dd2b5f09-92f4-4711-8e96-1222e030b33f

About this result

Related concepts (29)

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.

In vivo magnetic resonance spectroscopy

In vivo magnetic resonance spectroscopy (MRS) is a specialized technique associated with magnetic resonance imaging (MRI). Magnetic resonance spectroscopy (MRS), also known as nuclear magnetic resonance (NMR) spectroscopy, is a non-invasive, ionizing-radiation-free analytical technique that has been used to study metabolic changes in brain tumors, strokes, seizure disorders, Alzheimer's disease, depression, and other diseases affecting the brain. It has also been used to study the metabolism of other organs such as muscles.

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Excitation of Selected Proton Signals in NMR of Isotopically Labeled Macromolecules

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