Publication

Relaxation-induced violations of coherence transfer selection rules in nuclear magnetic resonance

Geoffrey Bodenhausen
1987
Journal Articles

Abstract

The effect of multiexponential transverse relaxation of degenerate transitions on coherence transfer phenomena in high-resoln. NMR is discussed. Dipolar relaxation of X3 and AX3 systems is considered, and the implications for multiple-quantum-filtered 2-dimensional correlation spectra of large mols. are analyzed. An expansion of the d. operator in terms of products of irreducible tensor operators is used for tracing the pathways of coherence transfer. [on SciFinder (R)]

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Geoffrey Bodenhausen
1987
Journal Articles

Abstract

Official source

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Nuclear magnetic resonance

Nuclear magnetic resonance (NMR) is a physical phenomenon in which nuclei in a strong constant magnetic field are perturbed by a weak oscillating magnetic field (in the near field) and respond by producing an electromagnetic signal with a frequency characteristic of the magnetic field at the nucleus. This process occurs near resonance, when the oscillation frequency matches the intrinsic frequency of the nuclei, which depends on the strength of the static magnetic field, the chemical environment, and the magnetic properties of the isotope involved; in practical applications with static magnetic fields up to ca.

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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 (4)

Relaxation-induced violations of coherence transfer selection rules in nuclear magnetic resonance

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