ACP-supported redeployment in response to the COVID-19 pandemic: a service evaluation of staff experience.

Background: During the COVID-19 pandemic, healthcare organisations around the world had to optimise resources and redeploy staff to meet unprecedented demands on services. This service evaluation aims to establish the experiences of nurses redeployed to a COVID-negative Nightingale ward during the first wave of the pandemic in the UK.

Methods: Purposive sampling using a survey was used to capture nurses' experiences.

Localising nuclear spins by pseudocontact shifts from a single tagging site.

Ligating a protein at a specific site with a tag molecule containing a paramagnetic metal ion provides a versatile way of generating pseudocontact shifts (PCSs) in nuclear magnetic resonance (NMR) spectra. PCSs can be observed for nuclear spins far from the tagging site, and PCSs generated from multiple tagging sites have been shown to enable highly accurate structure determinations at specific sites of interest, even when using flexible tags, provided the fitted effective magnetic susceptibility anisotropy () tensors accurately back-calculate the experimental PCSs measured in the immediate vicinity of the site of interest. The present work investigates the situation where only the local structure of a protein region or bound ligand is to be determined rather than the structure of the entire molecular system.

Paramagnetic Chemical Probes for Studying Biological Macromolecules.

Paramagnetic chemical probes have been used in electron paramagnetic resonance (EPR) and nuclear magnetic resonance (NMR) spectroscopy for more than four decades. Recent years witnessed a great increase in the variety of probes for the study of biological macromolecules (proteins, nucleic acids, and oligosaccharides). This Review aims to provide a comprehensive overview of the existing paramagnetic chemical probes, including chemical synthetic approaches, functional properties, and selected applications.

Localising individual atoms of tryptophan side chains in the metallo--lactamase IMP-1 by pseudocontact shifts from paramagnetic lanthanoid tags at multiple sites.

The metallo--lactamase IMP-1 features a flexible loop near the active site that assumes different conformations in single crystal structures, which may assist in substrate binding and enzymatic activity. To probe the position of this loop, we labelled the tryptophan residues of IMP-1 with 7-C-indole and the protein with lanthanoid tags at three different sites. The magnetic susceptibility anisotropy () tensors were determined by measuring pseudocontact shifts (PCSs) of backbone amide protons.

Organoarsenic probes to study proteins by NMR spectroscopy.

Arsenical probes enable structural studies of proteins. We report the first organoarsenic probes for nuclear magnetic resonance (NMR) and electron paramagnetic resonance (EPR) spectroscopy to study proteins in solutions. These probes can be attached to irregular loop regions.