Publication

Highly selective excitation in biomolecular NMR by frequency-switched single-transition cross-polarization

Geoffrey Bodenhausen
2002
Journal Articles

Abstract

A new method for selective excitation in biomol. NMR uses two-fold single-transition cross-polarization between protons and nitrogen-15 or carbon-13 nuclei. Switching the frequencies between the forward and backward transfer steps allows one to select a multiplet pattern that is assocd. with a single pair of spins in a medium-size protein. The efficiency of the transfer benefits from so-called TROSY line-narrowing effects which arise from interference between relaxation mechanisms. [on SciFinder (R)]

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https://infoscience.epfl.ch/entities/publication/34c59270-89e7-4759-9e59-cd69ebe2502f

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Geoffrey Bodenhausen
2002
Journal Articles

Abstract

Official source

https://infoscience.epfl.ch/entities/publication/34c59270-89e7-4759-9e59-cd69ebe2502f

About this result

Related concepts (24)

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.

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.

Protein folding

Protein folding is the physical process where a protein chain is translated into its native three-dimensional structure, typically a "folded" conformation, by which the protein becomes biologically functional. Via an expeditious and reproducible process, a polypeptide folds into its characteristic three-dimensional structure from a random coil. Each protein exists first as an unfolded polypeptide or random coil after being translated from a sequence of mRNA into a linear chain of amino acids.

Related publications (1)

Highly selective excitation in biomolecular NMR by frequency-switched single-transition cross-polarization

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Determination of relaxation pathways in coupled spin systems by two-dimensional NMR exchange spectroscopy with small flip angles