Publication

Longitudinal two-spin order in 2D exchange spectroscopy (NOESY)

Geoffrey Bodenhausen
1984
Journal Articles

Abstract

Attention is drawn to a class of signals that appear if the rotation angles of the radio-frequency pulses in the 2-dimensional (2D) exchange expt. are inadvertently or deliberately set to b!=p/2. The signals (zz signals) arise from longitudinal 2-spin order in the mixing period, and can be sepd. from genuine exchange signals by exploiting the characteristic response to a p pulse inserted in the mixing period. Pulse sequences are shown for (1) conventional 2D exchange spectroscopy, (2) a modified 2D exchange expt. for excitation and reconversion of longitudinal 2-spin order, and (3) suppression of zz signals in 2D exchange spectroscopy. The efficiency of the sepn. procedure is illustrated with NOESY spectra of the protein basic pancreatic trypsin inhibitor. [on SciFinder (R)]

Official source

https://infoscience.epfl.ch/entities/publication/ef7e9e18-b2be-4241-b4e7-9cc618442a78

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Geoffrey Bodenhausen
1984
Journal Articles

Abstract

Official source

https://infoscience.epfl.ch/entities/publication/ef7e9e18-b2be-4241-b4e7-9cc618442a78

About this result

Related concepts (29)

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.

Related publications (1)

Longitudinal two-spin order in 2D exchange spectroscopy (NOESY)

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