Metalloproteins constitute a significant fraction of the proteome all organisms and their characterization is critical for both basic sciences biomedical applications. A large portion metalloproteins bind paramagnetic metal ions, NMR spectroscopy has been widely used in structural characterization. However, signals nuclei immediate vicinity center are often broadened beyond detection. In this w...

Metalloproteins play important roles in biology. They account for about 1/3 of structurally characterized proteins and about 1/2 of all proteins.1 The availability of different metal ions with various redox states, ligands, and geometries about the metal ion allows for fine-tuning of the reactivity of proteins at the highest level. As shown in other sections of this encyclopedia, studies of nat...

In fluorophore-cored dendrimers with peripheral binding functionalities, the effect of generation upon protein binding-induced fluorescence quenching can be unpredictable; this is because the increase in fluorophore-binding functionality distance with generation is also accompanied by an increase in the number of binding moieties and the interplay between the two features is utilized to create ...

NMR experiments and tools for the characterization of the structure and dynamics of paramagnetic proteins are presented here. The focus is on the importance of (13)C direct-detection NMR for the assignment of paramagnetic systems in solution, on the information contained in paramagnetic effects observed both in solution and in the solid state, and on novel paramagnetism-based tools for the inve...