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Advances in Biomolecular EPR, Volume 666 in the Methods of Enzymology series, highlights new advances in the field, with this new volume presenting interesting chapters on topics including Magnetic Resonance Characterization of Physiologically Important Metal Ion Binding Sites in the Prion and Related Proteins, The catalytic role of metal-radical/protein-based radicals in heme enzymes, Rigid Cu2+-based spin labels for the study of higher-order DNA G-quadruplex structures, Orthogonal spin labeling and membrane proteins: increasing the information content and going towards in cell applications, Spectroscopic investigation of mono- and di-Mn-containing centers in biochemistry with an emphasis on application of paramagnetic resonance techniques, and more.
Additional chapters cover In Vivo pO2 Imaging of Tumors: Oxymetry with Very Low-Frequency Electron Paramagnetic Resonance, an Update, EPR contributions to understanding molybdenum-containing enzymes, EPR spectroscopy of Type I reaction centers, Characterization of a substrate-derived radical in the NosN reaction during the biosynthesis of nosiheptide, and much more.
List of contents
1. Magnetic Resonance Characterization of Physiologically Important Metal Ion Binding Sites in the Prion and Related Proteins
2. The catalytic role of metal-radical/protein-based radicals in heme enzymes
3. Rigid Cu2+-based spin labels for the study of higher-order DNA G-quadruplex structures
4. Orthogonal spin labeling and membrane proteins: increasing the information content and going towards in cell applications
5. Spectroscopic investigation of mono- and di-Mn-containing centers in biochemistry with an emphasis on application of paramagnetic resonance techniques
6. In Vivo pO2 Imaging of Tumors: Oxymetry with Very Low-Frequency Electron Paramagnetic Resonance, an Update
7. EPR contributions to understanding molybdenum-containing enzymes
8. EPR spectroscopy of Type I reaction centers
9. Characterization of a substrate-derived radical in the NosN reaction during the biosynthesis of nosiheptide
10. Functional solvent-protein interactions characterized by using spin probe EPR spectroscopy
11. Integrative Ensemble Modelling of Proteins and their Complexes with Distance Distribution Restraints
12. Site directed spin label probes of the mechanism of the cyanobacterial circadian clock
13. Pulsed EPR spectroscopy as a tool to probe non-canonical electronic structures in artificial metalloenzymes
14. Light-induced Pulsed Dipolar EPR Spectroscopy for distance and orientation analysis
15. Recent Advances in Dynamic Nuclear Polarization
16. Advances in Rapid Scan EPR Spectroscopy
17. Controlling and exploiting intrinsic unpaired electrons in metalloproteins
18. EPR advances in characterizing radical SAM Enzymology
19. Overhauser high field DNP
20. Experimental Guidelines for Trapping Paramagnetic Reaction Intermediates in Radical S-Adenosylmethionine Enzymes
21. EPR Characterization of Synthetic Structural and Functional Analogs of Metalloenzyme Active Sites
22. EPR spectroscopy on kinases
About the author
R. David Britt is the Winston Ko Chair and Distinguished Professor of Chemistry at the University of California, Davis. Prof. Britt uses electron paramagnetic resonance (EPR) spectroscopy to study metalloenzymes and enzymes containing organic radicals in their active sites.Britt is the recipient of multiple awards for his research, including the Bioinorganic Chemistry Award in 2019 and the Bruker Prize in 2015 from the Royal Society of Chemistry. He has received a Gold Medal from the International EPR Society (2014), and the Zavoisky Award from the Kazan Scientific Center of the Russian Academy of Sciences (2018).He is a Fellow of the American Association for the Advancement of Science and of the Royal Society of Chemistry.
