Publication

Identification of Spin Diffusion Pathways in Isotopically Labeled Biomolecules

Geoffrey Bodenhausen, Dominique Früh
1999
Journal Articles

Abstract

One-dimensional NOE expts. applicable to labeled macromols. are presented which allow the manipulation of specific spin diffusion pathways and thus unambiguously identify clandestine spins through which the direct NOE is mediated. A treatment of spin diffusion using av. Liouvillian theory is shown to describe adequately these phenomena. Expts. are carried out on an 15N-labeled sample of human ubiquitin. (c) 1999 Academic Press. [on SciFinder (R)]

Official source

https://infoscience.epfl.ch/entities/publication/a76171ed-3676-4dd0-b41e-4b3c97758ee2

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Geoffrey Bodenhausen, Dominique Früh
1999
Journal Articles

Abstract

Official source

https://infoscience.epfl.ch/entities/publication/a76171ed-3676-4dd0-b41e-4b3c97758ee2

About this result

Related concepts (21)

Ubiquitin

Ubiquitin is a small (8.6 kDa) regulatory protein found in most tissues of eukaryotic organisms, i.e., it is found ubiquitously. It was discovered in 1975 by Gideon Goldstein and further characterized throughout the late 1970s and 1980s. Four genes in the human genome code for ubiquitin: UBB, UBC, UBA52 and RPS27A. The addition of ubiquitin to a substrate protein is called ubiquitylation (or, alternatively, ubiquitination or ubiquitinylation).

Ubiquitin ligase

A ubiquitin ligase (also called an E3 ubiquitin ligase) is a protein that recruits an E2 ubiquitin-conjugating enzyme that has been loaded with ubiquitin, recognizes a protein substrate, and assists or directly catalyzes the transfer of ubiquitin from the E2 to the protein substrate. In simple and more general terms, the ligase enables movement of ubiquitin from a ubiquitin carrier to another thing (the substrate) by some mechanism. The ubiquitin, once it reaches its destination, ends up being attached by an isopeptide bond to a lysine residue, which is part of the target protein.

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.