期刊
CHEMICAL REVIEWS
卷 122, 期 10, 页码 9422-9467出版社
AMER CHEMICAL SOC
DOI: 10.1021/acs.chemrev.1c00796
关键词
-
资金
- Swiss National Science Foundation (SNSF) [185388]
Paramagnetic centers, such as metal ions bound to proteins, can affect the nuclei in their surroundings through the pseudocontact shift (PCS). PCS provides spatial information and can be used to characterize the structure, function, and dynamics of biomolecules. It has various applications, including structure refinement, magnifying dynamics, resonance assignments, intermolecular positioning, and structural information under sensitivity-limited situations. This review discusses the applications of PCS in biomolecular solution NMR spectroscopy and emphasizes its potential in structural biology.
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 A 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.
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