Pseudocontact Shifts in Biomolecular NMR Spectroscopy
| Autor: | Thomas Müntener, Daniel Joss, Daniel Häussinger, Sebastian Hiller |
|---|---|
| Rok vydání: | 2022 |
| Předmět: | |
| Zdroj: | Chemical Reviews. 122:9422-9467 |
| ISSN: | 1520-6890 0009-2665 |
| DOI: | 10.1021/acs.chemrev.1c00796 |
| Popis: | 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 pseudocontact shift (PCS), which leads to strong chemical shift perturbations of nuclear spins, with a remarkably long range of 50 Å and beyond. The PCS in solution NMR is an effect originating from the anisotropic part of the dipole-dipole interaction between the magnetic momentum of unpaired electrons and nuclear spins. The PCS contains spatial information that can be exploited in multiple ways to characterize structure, function, and dynamics of biomacromolecules. It can be used to refine structures, magnify effects of dynamics, help resonance assignments, allows for an intermolecular positioning system, and gives structural information in sensitivity-limited situations where all other methods fail. Here, we review applications of the PCS in biomolecular solution NMR spectroscopy, starting from early works on natural metalloproteins, following the development of non-natural tags to chelate and attach lanthanoid ions to any biomolecular target to advanced applications on large biomolecular complexes and inside living cells. We thus hope to not only highlight past applications but also shed light on the tremendous potential the PCS has in structural biology. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|