Publication

A spectral window in protein NMR revealing cross-relaxation between amide protons

Geoffrey Bodenhausen
1998
Journal Articles

Abstract

The principle of quenching undesirable indirect external trouble in nuclear Overhauser effect spectroscopy (QUIET-NOESY) relies on a doubly selective inversion of the longitudinal magnetization components of a source spin A and a target spin X to measure the cross-relaxation rate (Overhauser effect) between A and X without significant perturbation by spin diffusion. In 15N-enriched proteins, this can be achieved by using a bilinear rotation decoupling (BIRD) sequence for the selective inversion of amide protons that have a scalar coupling to nitrogen-15. The procedure can be improved by using editing techniques to simplify the resulting NOESY spectra. [on SciFinder (R)]

Official source

https://infoscience.epfl.ch/entities/publication/955385cd-3df6-45dc-9fb6-15ff098b4fef

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Geoffrey Bodenhausen
1998
Journal Articles

Abstract

Official source

https://infoscience.epfl.ch/entities/publication/955385cd-3df6-45dc-9fb6-15ff098b4fef

About this result

Related concepts (32)

Nuclear Overhauser effect

The nuclear Overhauser effect (NOE) is the transfer of nuclear spin polarization from one population of spin-active nuclei (e.g. 1H, 13C, 15N etc.) to another via cross-relaxation. A phenomenological definition of the NOE in nuclear magnetic resonance spectroscopy (NMR) is the change in the integrated intensity (positive or negative) of one NMR resonance that occurs when another is saturated by irradiation with an RF field. The change in resonance intensity of a nucleus is a consequence of the nucleus being close in space to those directly affected by the RF perturbation.

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.

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A spectral window in protein NMR revealing cross-relaxation between amide protons

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