Assessing Induced Folding of an Intrinsically Disordered Protein by Site-Directed Spin-Labeling Electron Paramagnetic Resonance Spectroscopy

2006 ◽  
Vol 110 (41) ◽  
pp. 20596-20608 ◽  
Author(s):  
Benjamin Morin ◽  
Jean-Marie Bourhis ◽  
Valérie Belle ◽  
Mireille Woudstra ◽  
Frédéric Carrière ◽  
...  
Keyword(s):  
Electron Paramagnetic Resonance Spectroscopy ◽  
Intrinsically Disordered Protein ◽  
Spin Labeling ◽  
Resonance Spectroscopy ◽  
Paramagnetic Resonance ◽  
Intrinsically Disordered ◽  
Disordered Protein ◽  
Induced Folding ◽  
Site Directed Spin Labeling ◽  
Electron Paramagnetic

Investigating Functional DNA Grafted on Nanodiamond Surface Using Site-Directed Spin Labeling and Electron Paramagnetic Resonance Spectroscopy

2016 ◽  
Vol 120 (17) ◽  
pp. 4003-4008 ◽  
Author(s):  
Rana D. Akiel ◽  
Xiaojun Zhang ◽  
Chathuranga Abeywardana ◽  
Viktor Stepanov ◽  
Peter Z. Qin ◽  
...  
Keyword(s):  
Electron Paramagnetic Resonance ◽  
Electron Paramagnetic Resonance Spectroscopy ◽  
Spin Labeling ◽  
Resonance Spectroscopy ◽  
Paramagnetic Resonance ◽  
Functional Dna ◽  
Site Directed Spin Labeling ◽  
Electron Paramagnetic

scholarly journals Monitoring the autoproteolysis of hiv-1 protease by site-directed spin-labeling and electron paramagnetic resonance spectroscopy

2011 ◽  
Vol 02 (02) ◽  
pp. 137-146 ◽  
Author(s):  
Jamie L. Kear ◽  
Luis Galiano ◽  
Angelo M. Veloro ◽  
Laura S. Busenlehner ◽  
Gail E. Fanucci
Keyword(s):  
Electron Paramagnetic Resonance ◽  
Electron Paramagnetic Resonance Spectroscopy ◽  
Spin Labeling ◽  
Resonance Spectroscopy ◽  
Paramagnetic Resonance ◽  
Site Directed Spin Labeling ◽  
Electron Paramagnetic ◽  
Hiv 1

scholarly journals Site Selective and Efficient Spin Labeling of Proteins with a Maleimide-Functionalized Trityl Radical for Pulsed Dipolar EPR Spectroscopy

Molecules ◽  
2019 ◽  
Vol 24 (15) ◽  
pp. 2735 ◽  
Author(s):  
J. Jacques Jassoy ◽  
Caspar A. Heubach ◽  
Tobias Hett ◽  
Frédéric Bernhard ◽  
Florian R. Haege ◽  
...  
Keyword(s):  
Electron Paramagnetic Resonance ◽  
Electron Paramagnetic Resonance Spectroscopy ◽  
Spin Labeling ◽  
Single Frequency ◽  
Spin Labels ◽  
Resonance Spectroscopy ◽  
Paramagnetic Resonance ◽  
Site Directed Spin Labeling ◽  
Site Selective ◽  
Electron Paramagnetic

Pulsed dipolar electron paramagnetic resonance spectroscopy (PDS) in combination with site-directed spin labeling (SDSL) of proteins and oligonucleotides is a powerful tool in structural biology. Instead of using the commonly employed gem-dimethyl-nitroxide labels, triarylmethyl (trityl) spin labels enable such studies at room temperature, within the cells and with single-frequency electron paramagnetic resonance (EPR) experiments. However, it has been repeatedly reported that labeling of proteins with trityl radicals led to low labeling efficiencies, unspecific labeling and label aggregation. Therefore, this work introduces the synthesis and characterization of a maleimide-functionalized trityl spin label and its corresponding labeling protocol for cysteine residues in proteins. The label is highly cysteine-selective, provides high labeling efficiencies and outperforms the previously employed methanethiosulfonate-functionalized trityl label. Finally, the new label is successfully tested in PDS measurements on a set of doubly labeled Yersinia outer protein O (YopO) mutants.

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