Publication

Triple-quantum NMR by selective triple resonance

Geoffrey Bodenhausen
1994
Journal Articles

Abstract

In high-resoln. NMR spectra of scalar coupled spins in isotropic phase, it is possible to convert single- into triple-quantum coherences and vice versa by irradiating simultaneously at the frequencies of 3 chem. shifts. A triple resonance condition can be achieved by modulating a radiofrequency carrier by a product of 2 cosinusoidal audiowaves, chosen so that 3 of the 4 sidebands coincide with 3 selected chem. shifts. When used in conjunction with 2-dimensional Fourier transform spectroscopy, it is possible to obtain triple-quantum multiplets with very high resoln. within a limited time span. The linewidths can give an accurate measure of the relaxation rates of triple-quantum coherences. [on SciFinder (R)]

Official source

https://infoscience.epfl.ch/entities/publication/45725d95-1bf7-447d-8a84-bbbbb0b64c81

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Geoffrey Bodenhausen
1994
Journal Articles

Abstract

Official source

https://infoscience.epfl.ch/entities/publication/45725d95-1bf7-447d-8a84-bbbbb0b64c81

About this result

Related concepts (24)

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.

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Triple-quantum NMR by selective triple resonance

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