Publication

Resolution enhancement in heteronuclear two-dimensional spectroscopy of realignment of coherence transfer echoes

Geoffrey Bodenhausen
1982
Journal Articles

Abstract

The resoln. in heteronuclear 2-dimensional NMR spectroscopy is affected by coherence transfer echoes. By introducing a delay between the transfer of coherence and the signal observation, the resoln. in the crucial w1 dimension can be enhanced. This procedure removes the symmetry of the multiplet structure, and an addnl. pulse is required to realign the signals in the 2-dimensional spectra. The methods are illustrated by applications to the indirect observation of scalar proton-proton couplings through P-31 in phosphothreonine. [on SciFinder (R)]

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https://infoscience.epfl.ch/entities/publication/e23b350c-60ed-44cf-a224-e1d70e40ffd5

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Geoffrey Bodenhausen
1982
Journal Articles

Abstract

Official source

https://infoscience.epfl.ch/entities/publication/e23b350c-60ed-44cf-a224-e1d70e40ffd5

About this result

Related concepts (26)

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.

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.

Related publications (13)

Resolution enhancement in heteronuclear two-dimensional spectroscopy of realignment of coherence transfer echoes

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