Abstract
Long-range structural information provided by the paramagnetic lanthanide probe methods is invaluable in the structural analysis of proteins, particularly protein complexes and multi-domain proteins. The application of paramagnetic lanthanide probe methods in protein structural analysis is expanding, owing to recent developments in lanthanide-binding tags. Here, we describe paramagnetic effects observed in the presence of paramagnetic lanthanide ions, which can be exploited to obtain structural information about proteins. We also illustrate practical aspects of the experiments and analyses utilizing the paramagnetic lanthanide probe methods. Applications in structure determination of protein–protein complexes and visualization of conformational changes in multi-domain proteins are also described.
Keywords
Fuyuhiko Inagaki: Deceased.
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Acknowledgements
We would like to thank Dr. Yoshihiro Kobashigawa for providing the data for Fig. 8.4 and Dr. Hiromasa Yagi for helpful comments and careful reading of the manuscript. A part of this work was supported by Creation of Innovation Centers for Advanced Interdisciplinary Research Areas Program, Ministry of Education, Culture, Sports, Science and Technology, Japan. This work was also partly supported by JSPS KAKENHI Grant Number 15H01624 and 15K20829 and by JST, PRESTO.
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Saio, T., Inagaki, F. (2018). Structural Study of Proteins by Paramagnetic Lanthanide Probe Methods. In: The Nuclear Magnetic Resonance Society of Japan (eds) Experimental Approaches of NMR Spectroscopy. Springer, Singapore. https://doi.org/10.1007/978-981-10-5966-7_8
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