Copper (Cu) is an essential trace element for all aerobic organisms. It functions as a cofactor
in enzymes that catalyze a wide variety of redox reactions due to its ability to cycle between …

Biological copper is coordinated predominantly by just three ligand types: the side chains of
histidine, cysteine, and methionine, with of course some exceptions. The arrangement of …

Nuclear magnetic resonance (NMR) is widely used across many fields of science because
of the rich data it produces, and some of the most valuable data come from studies of …

Paramagnetic centers in biomolecules, such as specific metal ions that are bound to a
protein, affect the nuclei in their surrounding in various ways. One of these effects is the …

1.1 Background The use of copper in biological systems coincides with the advent of an
oxygen atmosphere about 1.7 billion years ago. The presence of O 2 both allowed the …

This article deals with the solution structure determination of paramagnetic metalloproteins
by NMR spectroscopy. These proteins were believed not to be suitable for NMR …

Thanks to recent improvements in NMR spectrometer hardware and pulse sequence design,
modern 13C NMR has become a useful tool for biomolecular applications. The complete …

The NMR determination of the structure of large biological macromolecules in solution is
primarily limited by the fast transverse relaxation that broadens lines and reduces spectral …

Recent findings suggest that both host and pathogen manipulate copper content in infected
host niches during infections. In this review, we summarize recent developments that …

Natively unfolded proteins are increasingly recognized to play important physiological roles.
These proteins do not crystallize, so NMR is the only technique able to provide structural …