Orientation-Selective DEER Using Rigid Spin Labels, Cofactors, Metals, and Clusters

2013 ◽  
pp. 283-327 ◽  
Author(s):  
Alice M. Bowen ◽  
Claudia E. Tait ◽  
Christiane R. Timmel ◽  
Jeffrey R. Harmer
Keyword(s):  
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.

scholarly journals Studies of transmembrane peptides by pulse dipolar spectroscopy with semi-rigid TOPP spin labels

2021 ◽  
Author(s):  
Igor Tkach ◽  
Ulf Diederichsen ◽  
Marina Bennati
Keyword(s):  
Molecular Level ◽  
Dipolar Interaction ◽  
Spin Labels ◽  
Paramagnetic Centers ◽  
Structural Adaptation ◽  
Paramagnetic Resonance ◽  
Transmembrane Peptides ◽  
Distance Distributions ◽  
Lipid Environment ◽  
Electron Paramagnetic

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

α-Synuclein Association with Phosphatidylglycerol Probed by Lipid Spin Labels†

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

Probing of sulfhydryl groups in the adenosine 5'-diphosphate/adenosine 5'-triphosphate carrier by maleimide spin-labels

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

Characteristics of Gd(III) spin labels for the study of protein conformations

2021 ◽  
Author(s):  
Angeliki Giannoulis ◽  
Yasmin Ben-Ishay ◽  
Daniella Goldfarb
Keyword(s):  
Spin Labels ◽  
Protein Conformations

Spin Label Study of Apomembranes and Purple Membranes

1993 ◽  
Vol 48 (5-6) ◽  
pp. 500-503
Author(s):  
Tzvetana R. Lazarova ◽  
Maya Y. Velitchkova
Keyword(s):  
Fatty Acids ◽  
Lipid Bilayer ◽  
Spin Label ◽  
Hyperfine Splitting ◽  
Esr Spectra ◽  
Spin Labels ◽  
Label Study ◽  
Splitting Parameter ◽  
Induced Changes ◽  
Purple Membranes

Abstract Three spin-labelled fatty acids were used to detect the dynamics of lipid bilayer of apomem branes and purple membranes. It was found that ESR spectra of spin labels bound to apo­ membranes showed a temperature-induced changes rather similar to those seen with purple membranes. At the same time, however, the values of hyperfine splitting parameter 2Tm were lower as compared to purple membranes. The results pointed out that the removal of the retinal from purple membranes affects the dynamics of lipid bilayer and apomembranes were more rigid structure than those of purple membranes.

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