Publication

Correlation of chemical shifts of protons and carbon-13

Geoffrey Bodenhausen
1978
Journal Articles

Abstract

A 2-dimensional Fourier-transform technique, involving the transfer of nuclear magnetization between protons and 13C, was used to correlate the NMR chem. shifts for directly-bonded protons and 13C. Illustrative spectra are presented for the Me-group regions of menthone and camphor with natural-abundance 13C. The 2-dimensional spectra of geminal di-Me groups show a characteristic pattern involving addnl. magnetization transfer through the long-range coupling J(C-C-Me). [on SciFinder (R)]

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https://infoscience.epfl.ch/entities/publication/f15d81a3-11d7-492a-9a8c-30920242047e

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Geoffrey Bodenhausen
1978
Journal Articles

Abstract

Official source

https://infoscience.epfl.ch/entities/publication/f15d81a3-11d7-492a-9a8c-30920242047e

About this result

Related concepts (28)

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.

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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Correlation of chemical shifts of protons and carbon-13

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