AI Article Synopsis
- Metalloproteins are crucial components of the proteome across all organisms, and understanding them is important for scientific research and medical advancements.
- Many metalloproteins interact with paramagnetic metal ions, making paramagnetic NMR spectroscopy a key method for studying their structure, although this technique often faces challenges due to signal broadening near metal centers.
- The research presented demonstrates a novel method to accurately determine the coordination environment of the paramagnetic metal in proteins by using a diamagnetic analogue as a reference and applying quantum chemical calculations to refine the geometry based on experimental data.
Article Abstract
Metalloproteins constitute a significant fraction of the proteome of all organisms and their characterization is critical for both basic sciences and biomedical applications. A large portion of metalloproteins bind paramagnetic metal ions, and paramagnetic NMR spectroscopy has been widely used in their structural characterization. However, the signals of nuclei in the immediate vicinity of the metal center are often broadened beyond detection. In this work, we show that it is possible to determine the coordination environment of the paramagnetic metal in the protein at a resolution inaccessible to other techniques. Taking the structure of a diamagnetic analogue as a starting point, a geometry optimization is carried out by fitting the pseudocontact shifts obtained from first principles quantum chemical calculations to the experimental ones.
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| http://dx.doi.org/10.1002/anie.202101149 | DOI Listing |
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