ChemInform Abstract: Synthesis of Spin Labels for ESR Imaging of Living Rat Head.

ChemInform ◽  
2010 ◽  
Vol 28 (43) ◽  
pp. no-no
Author(s):  
R. NIWA ◽  
R. KONAKA ◽  
M. HIRAMATSU ◽  
H. KAMADA
Keyword(s):  
1997 ◽  
Vol 45 (5) ◽  
pp. 923-927 ◽  
Author(s):  
Ryuji NIWA ◽  
Ryusei KONAKA ◽  
Midori HIRAMATSU ◽  
Hitoshi KAMADA
Keyword(s):  

Author(s):  
Hannah Russell ◽  
Rachel Stewart ◽  
Christopher Prior ◽  
Vasily S. Oganesyan ◽  
Thembaninkosi G. Gaule ◽  
...  

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.


Author(s):  
Igor Tkach ◽  
Ulf Diederichsen ◽  
Marina Bennati

AbstractElectron paramagnetic resonance (EPR)-based pulsed dipolar spectroscopy measures the dipolar interaction between paramagnetic centers that are separated by distances in the range of about 1.5–10 nm. Its application to transmembrane (TM) peptides in combination with modern spin labelling techniques provides a valuable tool to study peptide-to-lipid interactions at a molecular level, which permits access to key parameters characterizing the structural adaptation of model peptides incorporated in natural membranes. In this mini-review, we summarize our approach for distance and orientation measurements in lipid environment using novel semi-rigid TOPP [4-(3,3,5,5-tetramethyl-2,6-dioxo-4-oxylpiperazin-1-yl)-L-phenylglycine] labels specifically designed for incorporation in TM peptides. TOPP labels can report single peak distance distributions with sub-angstrom resolution, thus offering new capabilities for a variety of TM peptide investigations, such as monitoring of various helix conformations or measuring of tilt angles in membranes. Graphical Abstract


Biochemistry ◽  
2003 ◽  
Vol 42 (44) ◽  
pp. 12919-12926 ◽  
Author(s):  
Muthu Ramakrishnan ◽  
Poul H. Jensen ◽  
Derek Marsh
Keyword(s):  

Biochemistry ◽  
1987 ◽  
Vol 26 (26) ◽  
pp. 8637-8644 ◽  
Author(s):  
Anton Munding ◽  
Michael Drees ◽  
Klaus Beyer ◽  
Martin Klingenberg

1996 ◽  
Vol 113 (3) ◽  
pp. 256-261 ◽  
Author(s):  
I. Nicholson ◽  
M.A. Foster ◽  
F.J.L. Robb ◽  
J.M.S. Hutchison ◽  
D.J. Lurie

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