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• W3161781161 abstract "The study of ever more complex biomolecular assemblies implicated in human health and disease is facilitated by a suite of complementary biophysical methods. Pulse dipolar electron paramagnetic resonance spectroscopy (PDS) is a powerful tool that provides highly precise geometric constraints in frozen solutions; however, the drive toward PDS at physiologically relevant sub-μM concentrations is limited by the currently achievable concentration sensitivity. Recently, PDS using a combination of nitroxide- and CuII-based spin labels allowed measuring a 500 nM concentration of a model protein. Using commercial instrumentation and spin labels, we demonstrate CuII-CuII and nitroxide-nitroxide PDS measurements at protein concentrations below previous examples reaching 500 and 100 nM, respectively. These results demonstrate the general feasibility of sub-μM PDS measurements at short to intermediate distances (∼1.5 to 3.5 nm), and are of particular relevance for applications where the achievable concentration is limiting." @default.
• W3161781161 created "2021-05-24" @default.
• W3161781161 creator A5078548237 @default.
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• W3161781161 date "2021-05-17" @default.
• W3161781161 modified "2023-10-15" @default.
• W3161781161 title "Nanomolar Pulse Dipolar EPR Spectroscopy in Proteins: Cu^II–Cu^II and Nitroxide–Nitroxide Cases" @default.
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• W3161781161 doi "https://doi.org/10.1021/acs.jpcb.1c03666" @default.
• W3161781161 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/7611071" @default.
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• W3161781161 hasPublicationYear "2021" @default.
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