The site specific incorporation of paramagnetic lanthanides to proteins produces a number of unique effects on the resulting NMR spectra of the protein, including paramagnetic relaxation enhancement, residual dipolar coupling and pseudo-contact shifts. These effects can be measured and quantified to yield valuable long range distance and angular restraints that can be utilized in protein NMR structure investigations.^1,2 Most proteins however are not inherently able to bind lanthanides, which has historically limited the use of these restraints to metalloproteins in which the native metal can be substituted for a paramagnetic lanthanide. In order to increase the range of proteins that can make use of these restraints, synthetic lanthanide binding tags capable of site specific conjugation to proteins have been developed. This project aims to develop novel lanthanide binding tags with improved properties to existing ones. The designed tags are capable of chelating lanthanides as highly stable polydentate complexes, preventing the need for addition of free lanthanide metals to protein samples. The tags are smaller than previously designed tags that are also able to tightly bind lanthanides, reducing the chances of affecting the protein's native structure. The tags are designed to be more hydrophilic in nature with improved water solubility compared to existing tags. Furthermore, the tags utilize very short linkers between the lanthanide and protein to impart rigidity and produce large paramagnetic effects. The synthesized tags have been assessed by conjugation to Ubiquitin as a model protein, with results showing significantly larger paramagnetic effects than a currently utilized tag.