Publication

Up to 16% Optical Carbon‐13 Hyperpolarization of Donor–Acceptor Molecules at 14.1 T

2026

Abstract

Solid‐state nuclear magnetic resonance (NMR) is a powerful technique for structure determination with applications ranging from biology to material sciences. However, its inherent low sensitivity prevents many applications. In solids, optical hyperpolarization techniques such as solid‐state photochemically induced dynamic nuclear polarization (photo‐CIDNP) could alleviate this limitation, by generating nuclear spin hyperpolarization. We recently showed that 1 H and 13 C photo‐CIDNP can be observed for synthetic donor–acceptor (D–A) molecules. However, polarization levels in these systems are so far relatively low (

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https://infoscience.epfl.ch/entities/publication/8289b5aa-1309-4e9d-8911-46cd5facd0ce

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2026

Abstract

Official source

https://infoscience.epfl.ch/entities/publication/8289b5aa-1309-4e9d-8911-46cd5facd0ce

About this result

Related concepts (32)

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.

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.

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 (22)

Up to 16% Optical Carbon‐13 Hyperpolarization of Donor–Acceptor Molecules at 14.1 T

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