Publication

Double resonance in heteronuclear two-dimensional spectroscopy

Geoffrey Bodenhausen
1981
Journal Articles

Abstract

Selective proton decoupling was used to remove one of the homonuclear splittings in heteronuclear 2-dimensional NMR. The addnl. effort required to adjust the decoupler frequency to one of the proton shifts is easily offset by the increased simplicity of the spectra. In the expt., continuous weak irradn. is applied at the chem. shift of one of the distant protons which is not directly coupled to the P nuclei. The carrier frequency of both proton pulses and selective irradn. is chosen to be one and the same. [on SciFinder (R)]

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Geoffrey Bodenhausen
1981
Journal Articles

Abstract

Official source

https://infoscience.epfl.ch/entities/publication/c0315b45-8b6c-46df-8681-b063682498b6

About this result

Related concepts (26)

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.

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 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 (14)

Double resonance in heteronuclear two-dimensional spectroscopy

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