EPR Techniques, Spin Labeling, and Spin Trapping

Sahu, Indra D.; Lorigan, Gary A.

doi:10.1016/b978-0-12-409547-2.14080-6

Cited by 4 publications

(6 citation statements)

References 136 publications

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“…In the following sections, we will discuss it in an introductory fashion with recent examples. For more in-depth information, we refer the following excellent reviews [12,13,42,47,50,[54][55][56][57][58]. extended the application of EPR spectroscopy to nearly any biological system.…”

Section: Nitroxide Based Site-directed Spin Labeling Epr For Studying Membrane Proteinsmentioning

confidence: 99%

“…Nitroxide-based SDSL EPR power saturation experiments can be used to study the topology of the protein with respect to the membrane [13,57,64,65,70]. There are several biologically important protein systems such as Escherichia coli ferric citrate transporter FecA, vimentin, GM2 activator protein, ABC cassette transporter MsbA, cytochrome C oxidase subunit IV (COX IV), the prokaryotic potassium channel KcsA, KCNQ1-VSD, Pinholin, KCNE1, lactose permease protein, integrin β 1a , functional amyloid Obr2A, C99 domain of the amyloid precursor protein, bacteriorhodopsin, KvAP voltage-sensing domain and phospholamban (PLB), and the GTPase domain of HydF that have been studied using nitroxide-based SDSL CW-EPR spectroscopy to probe the structural, topology, and dynamic properties [51,60,62,65,66,[70][71][72][73][74][75][76][77][78][79][80][81][82][83][84][85].…”

Section: Sdsl Cw-epr For Studying Structural Topology and Dynamic Properties Of Membrane Proteinsmentioning

confidence: 99%

“…In DEER spectroscopy, a dipolar coupling between two spins is measured by monitoring one set of spins while exciting another set of spins with a second microwave frequency, leading to the measurement of the distance between them [36,128,131]. Nitroxide spin labeling based DEER spectroscopy is very popular for investigating the secondary, tertiary, and quaternary structures and conformational dynamics of a wide variety of macromolecules [19,44,57,61,[120][121][122][123][124][125][126][127][128][129][130][132][133][134][135][136][137]. In addition to nitroxide spin labels, other spin labels such as functionalized chelators of paramagnetic lanthanides (Gd III ), carbon-based radicals (trityl), and metals such as copper (Cu II ) have been recently utilized for DEER measurements on membrane proteins [56,[138][139][140][141].…”

Section: Double Electron Electron Resonance (Deer) Techniques For Distance Measurementsmentioning

confidence: 99%

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Electron Paramagnetic Resonance as a Tool for Studying Membrane Proteins

Sahu

Lorigan

2020

Biomolecules

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Membrane proteins possess a variety of functions essential to the survival of organisms. However, due to their inherent hydrophobic nature, it is extremely difficult to probe the structure and dynamic properties of membrane proteins using traditional biophysical techniques, particularly in their native environments. Electron paramagnetic resonance (EPR) spectroscopy in combination with site-directed spin labeling (SDSL) is a very powerful and rapidly growing biophysical technique to study pertinent structural and dynamic properties of membrane proteins with no size restrictions. In this review, we will briefly discuss the most commonly used EPR techniques and their recent applications for answering structure and conformational dynamics related questions of important membrane protein systems.

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Section: Nitroxide Based Site-directed Spin Labeling Epr For Studying Membrane Proteinsmentioning

confidence: 99%

Section: Sdsl Cw-epr For Studying Structural Topology and Dynamic Properties Of Membrane Proteinsmentioning

confidence: 99%

Section: Double Electron Electron Resonance (Deer) Techniques For Distance Measurementsmentioning

confidence: 99%

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Electron Paramagnetic Resonance as a Tool for Studying Membrane Proteins

Sahu

Lorigan

2020

Biomolecules

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“…In contrast, radical 7 exhibited a five-line spectrum centered at g = 2.0034, close to the value of the free electron. The hyperfine splitting comes from the interaction of the radical with two equivalent 14 N nuclei, with coupling constant and bandwidth of a = 6.5 G and Δ H pp = 3.1 G, respectively …”

Section: Resultsmentioning

confidence: 99%

Efficient Routes for the Preparation of Urazole Radical Self-Assembled Monolayers on Gold Surfaces

et al. 2022

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The functionalization of substrates with radical species has been shown to be a promising strategy to confer novel physical and chemical properties to a surface. Urazole radicals are persistent nitrogen-centered radicals that are insensitive to oxygen, making them desirable targets for the functionalization of surfaces. Here, we succeed in the preparation of self-assembled monolayers (SAMs) of a 1-arylurazole radical on Au surfaces using two different approaches. In the first approach, a SAM of a radical precursor on the gold surface is prepared followed by its chemical oxidation to generate the active urazole radical. In the second route, the radical is generated in solution and subsequently grafted on the Au surface. In both cases, the SAMs exhibit active radical behavior, but the SAM prepared by the first approach demonstrates greater surface coverage of the electroactive urazole radical species.

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“…Nitroxide spin labeling based SDSL DEER spectroscopy is a widely used biophysical technique for studying secondary, tertiary and quaternary structures, and conformational dynamics of a numerous membrane proteins [6,11,32,41,83,98,[104][105][106][107][108][109][110]. However, other spin labels including functionalized chelators of paramagnetic lanthanides (Gd III ), carbonbased radicals ((trityl), and metals such as copper (Cu II ) have been recently applied for DEER experiments for studying membrane proteins [111][112][113][114][115][116].…”

Section: Site Directed Spin Labeling (Sdsl) Approaches For Epr Spectrmentioning

confidence: 99%

Probing Structural Dynamics of Membrane Proteins Using Electron Paramagnetic Resonance Spectroscopic Techniques

Sahu

Lorigan

2021

Biophysica

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Membrane proteins are essential for the survival of living organisms. They are involved in important biological functions including transportation of ions and molecules across the cell membrane and triggering the signaling pathways. They are targets of more than half of the modern medical drugs. Despite their biological significance, information about the structural dynamics of membrane proteins is lagging when compared to that of globular proteins. The major challenges with these systems are low expression yields and lack of appropriate solubilizing medium required for biophysical techniques. Electron paramagnetic resonance (EPR) spectroscopy coupled with site directed spin labeling (SDSL) is a rapidly growing powerful biophysical technique that can be used to obtain pertinent structural and dynamic information on membrane proteins. In this brief review, we will focus on the overview of the widely used EPR approaches and their emerging applications to answer structural and conformational dynamics related questions on important membrane protein systems.

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EPR Techniques, Spin Labeling, and Spin Trapping

Cited by 4 publications

References 136 publications

Electron Paramagnetic Resonance as a Tool for Studying Membrane Proteins

Electron Paramagnetic Resonance as a Tool for Studying Membrane Proteins

Efficient Routes for the Preparation of Urazole Radical Self-Assembled Monolayers on Gold Surfaces

Probing Structural Dynamics of Membrane Proteins Using Electron Paramagnetic Resonance Spectroscopic Techniques

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