Site-Specific Incorporation of Nitroxide Spin-Labels into Internal Sites of the TAR RNA; Structure-Dependent Dynamics of RNA by EPR Spectroscopy

2001 ◽  
Vol 123 (7) ◽  
pp. 1527-1528 ◽  
Author(s):  
Thomas E. Edwards ◽  
Tamara M. Okonogi ◽  
Bruce H. Robinson ◽  
Snorri Th. Sigurdsson
Keyword(s):  
Epr Spectroscopy ◽  
Rna Structure ◽  
Spin Labels ◽  
Site Specific ◽  
Nitroxide Spin Labels ◽  
Tar Rna

Site-specific insertion of nitroxide-spin labels into DNA probes by click chemistry for structural analyses by ELDOR spectroscopy

2008 ◽  
Vol 52 (1) ◽  
pp. 147-148 ◽  
Author(s):  
M. Flaender ◽  
G. Sicoli ◽  
Th. Fontecave ◽  
G. Mathis ◽  
C. Saint-Pierre ◽  
...  
Keyword(s):  
Click Chemistry ◽  
Dna Probes ◽  
Spin Labels ◽  
Site Specific ◽  
Nitroxide Spin Labels

Site-specific incorporation of nitroxide spin-labels into 2′-positions of nucleic acids

2007 ◽  
Vol 2 (8) ◽  
pp. 1954-1962 ◽  
Author(s):  
Thomas E Edwards ◽  
Snorri Th Sigurdsson
Keyword(s):  
Nucleic Acids ◽  
Spin Labels ◽  
Site Specific ◽  
Nitroxide Spin Labels

scholarly journals DEER and RIDME Measurements of the Nitroxide-Spin Labelled Copper-Bound Amine Oxidase Homodimer from Arthrobacter Globiformis

2021 ◽  
Author(s):  
Hannah Russell ◽  
Rachel Stewart ◽  
Christopher Prior ◽  
Vasily S. Oganesyan ◽  
Thembaninkosi G. Gaule ◽  
...  
Keyword(s):  
Dipolar Coupling ◽  
Amine Oxidase ◽  
Spin Labels ◽  
Arthrobacter Globiformis ◽  
Copper Amine Oxidase ◽  
Dipole Interactions ◽  
Nitroxide Spin Labels ◽  
Double Electron Electron Resonance ◽  
Dipolar Modulation ◽  
Paramagnetic Centres

AbstractIn the study of biological structures, pulse dipolar spectroscopy (PDS) is used to elucidate spin–spin distances at nanometre-scale by measuring dipole–dipole interactions between paramagnetic centres. The PDS methods of Double Electron Electron Resonance (DEER) and Relaxation Induced Dipolar Modulation Enhancement (RIDME) are employed, and their results compared, for the measurement of the dipolar coupling between nitroxide spin labels and copper-II (Cu(II)) paramagnetic centres within the copper amine oxidase from Arthrobacter globiformis (AGAO). The distance distribution results obtained indicate that two distinct distances can be measured, with the longer of these at c.a. 5 nm. Conditions for optimising the RIDME experiment such that it may outperform DEER for these long distances are discussed. Modelling methods are used to show that the distances obtained after data analysis are consistent with the structure of AGAO.

Comparison of Ionic and Non-Ionic Nitroxide Spin Labels for Urographic Enhancement in Magnetic Resonance Imaging

1987 ◽  
Vol 28 (5) ◽  
pp. 593-600 ◽  
Author(s):  
Wolfgang Grodd ◽  
H. Paajanen ◽  
U. G. Eriksson ◽  
D. Revel ◽  
F. Terrier ◽  
...  
Keyword(s):  
Magnetic Resonance Imaging ◽  
Magnetic Resonance ◽  
Spin Labels ◽  
Resonance Imaging ◽  
Nitroxide Spin Labels

Characterization of Bifunctional Spin Labels for Investigating the Structural and Dynamic Properties of Membrane Proteins Using EPR Spectroscopy

2017 ◽  
Vol 121 (39) ◽  
pp. 9185-9195 ◽  
Author(s):  
Indra D. Sahu ◽  
Andrew F. Craig ◽  
Megan M. Dunagum ◽  
Robert M. McCarrick ◽  
Gary A. Lorigan
Keyword(s):  
Membrane Proteins ◽  
Epr Spectroscopy ◽  
Dynamic Properties ◽  
Spin Labels

Triplet Fullerenes as Prospective Spin Labels for Nanoscale Distance Measurements by Pulsed Dipolar EPR Spectroscopy

2019 ◽  
Vol 131 (38) ◽  
pp. 13405-13409 ◽  
Author(s):  
Olesya A. Krumkacheva ◽  
Ivan O. Timofeev ◽  
Larisa V. Politanskaya ◽  
Yuliya F. Polienko ◽  
Evgeny V. Tretyakov ◽  
...  
Keyword(s):  
Epr Spectroscopy ◽  
Spin Labels ◽  
Distance Measurements
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