Publication

Elimination of flip-angle effects in two-dimensional NMR spectroscopy. Application to cyclic nucleotides

Geoffrey Bodenhausen
1980
Journal Articles

Abstract

The proton and 31P NMR spectra of 2',3'-cyclic uridine monophosphate have been correlated by means of heteronuclear two-dimensional NMR. The spectra depend on the flip angle of one of the rf pulses. This is in contrast to previously reported applications where the 31P nucleus was coupled to a single proton only. For flip angles other than 90 Deg the spectra cannot be readily related to conventional proton spectra and the conformational information is obscured. The resulting multiplets can be analyzed by routine simulation techniques to ext. proton-proton coupling consts. This information, which can be related to the mol. conformation, is often not available from conventional proton spectra. [on SciFinder (R)]

Official source

https://infoscience.epfl.ch/entities/publication/52c91715-aa04-418c-b600-a090224a09ee

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Geoffrey Bodenhausen
1980
Journal Articles

Abstract

Official source

https://infoscience.epfl.ch/entities/publication/52c91715-aa04-418c-b600-a090224a09ee

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.

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.

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Elimination of flip-angle effects in two-dimensional NMR spectroscopy. Application to cyclic nucleotides

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