Results 1 to 10 of about 37,070 (307)

Spin-Lattice Relaxation Rates of Lipid Spin Labels as a Measure of Their Rotational Diffusion Rates in Lipid Bilayer Membranes [PDF]

open access: yesMembranes, 2022
The spin-lattice relaxation rate (T1−1) of lipid spin labels obtained from saturation recovery EPR measurements in deoxygenated membranes depends primarily on the rate of the rotational diffusion of the nitroxide moiety within the lipid bilayer.
Witold K. Subczynski, Justyna Widomska
doaj   +2 more sources

gem‐Diethyl Pyrroline Nitroxide Spin Labels: Synthesis, EPR Characterization, Rotamer Libraries and Biocompatibility [PDF]

open access: yesChemistryOpen, 2019
The availability of bioresistant spin labels is crucial for the optimization of site‐directed spin labeling protocols for EPR structural studies of biomolecules in a cellular context.
Dr. Stephanie Bleicken   +9 more
doaj   +4 more sources

New Developments in Spin Labels for Pulsed Dipolar EPR [PDF]

open access: yesMolecules, 2014
Spin labelling is a chemical technique that enables the integration of a molecule containing an unpaired electron into another framework for study. Given the need to understand the structure, dynamics, and conformational changes of biomacromolecules ...
Alistair J. Fielding   +3 more
doaj   +2 more sources

A Simple Method of Synthesis of 3-Carboxy-2,2,5,5-Tetraethylpyrrolidine-1-oxyl and Preparation of Reduction-Resistant Spin Labels and Probes of Pyrrolidine Series [PDF]

open access: yesMolecules, 2021
Stable free radicals are widely used as molecular probes and labels in various biophysical and biomedical research applications of magnetic resonance spectroscopy and imaging.
Sergey A. Dobrynin   +11 more
doaj   +2 more sources

A Comparison of Cysteine-Conjugated Nitroxide Spin Labels for Pulse Dipolar EPR Spectroscopy [PDF]

open access: yesMolecules, 2021
The structure-function and materials paradigms drive research on the understanding of structures and structural heterogeneity of molecules and solids from materials science to structural biology.
Katrin Ackermann   +2 more
doaj   +2 more sources

A new perspective on membrane-embedded Bax oligomers using DEER and bioresistant orthogonal spin labels [PDF]

open access: yesScientific Reports, 2019
Bax is a Bcl-2 protein crucial for apoptosis initiation and execution, whose active conformation is only partially understood. Dipolar EPR spectroscopy has proven to be a valuable tool to determine coarse-grained models of membrane-embedded Bcl-2 ...
Markus Teucher   +7 more
doaj   +2 more sources

Membrane Depth Measurements of E Protein by 2H ESEEM Spectroscopy in Lipid Bilayers [PDF]

open access: yesBiophysica
A topological analysis was performed by taking ESEEM measurements of site-specifically labeled E protein from SARS-CoV-2. The intensity of deuterium modulation arising from either deuterated solvent or deuterated lipid acyl chains revealed exposure to ...
Andrew K. Morris   +2 more
doaj   +2 more sources

Structural dynamics of calmodulin-ryanodine receptor interactions: electron paramagnetic resonance using stereospecific spin labels [PDF]

open access: yesScientific Reports, 2018
We have used electron paramagnetic resonance, with rigid and stereospecific spin labels, to resolve structural states in calmodulin (CaM), as affected by binding of Ca and a CaM-binding peptide (RyRp) derived from the ryanodine receptor (RyR), the Ca ...
Cheng Her   +3 more
doaj   +2 more sources

Strategies to identify and suppress crosstalk signals in double electron–electron resonance (DEER) experiments with gadoliniumIII and nitroxide spin-labeled compounds [PDF]

open access: yesMagnetic Resonance, 2020
Double electron–electron resonance (DEER) spectroscopy applied to orthogonally spin-labeled biomolecular complexes simplifies the assignment of intra- and intermolecular distances, thereby increasing the information content per sample.
M. Teucher   +5 more
doaj   +1 more source

Site-specific structural order in Alzheimer's Aβ42 fibrils [PDF]

open access: yesRoyal Society Open Science, 2018
Deposition of amyloid fibrils is a pathological hallmark of Alzheimer's disease. Aβ42 is the major protein whose aggregation leads to the formation of these fibrils.
Hongsu Wang   +3 more
doaj   +1 more source

Home - About - Disclaimer - Privacy