15 research outputs found
Electron spin coherence exceeding seconds in high purity silicon
Silicon is undoubtedly one of the most promising semiconductor materials for
spin-based information processing devices. Its highly advanced fabrication
technology facilitates the transition from individual devices to large-scale
processors, and the availability of an isotopically-purified Si form
with no magnetic nuclei overcomes what is a main source of spin decoherence in
many other materials. Nevertheless, the coherence lifetimes of electron spins
in the solid state have typically remained several orders of magnitude lower
than what can be achieved in isolated high-vacuum systems such as trapped ions.
Here we examine electron spin coherence of donors in very pure Si
material, with a residual Si concentration of less than 50 ppm and donor
densities of per cm. We elucidate three separate mechanisms
for spin decoherence, active at different temperatures, and extract a coherence
lifetime up to 2 seconds. In this regime, we find the electron spin is
sensitive to interactions with other donor electron spins separated by ~200 nm.
We apply a magnetic field gradient in order to suppress such interactions and
obtain an extrapolated electron spin of 10 seconds at 1.8 K. These
coherence lifetimes are without peer in the solid state by several orders of
magnitude and comparable with high-vacuum qubits, making electron spins of
donors in silicon ideal components of a quantum computer, or quantum memories
for systems such as superconducting qubits.Comment: 18 pages, 4 figures, supplementary informatio
DEER Distance Measurements on Proteins
ISSN:0066-426XISSN:1545-159
EPR Techniques to Probe Insertion and Conformation of Spin-Labeled Proteins in Lipid Bilayers
Electron paramagnetic resonance (EPR) spectroscopy of spin-labeled membrane proteins is a valuable biophysical technique to study structural details and conformational transitions of proteins close to their physiological environment, for example, in liposomes, membrane bilayers, and nanodiscs. Unlike in nuclear magnetic resonance (NMR) spectroscopy, having only one or few specific side chains labeled at a time with paramagnetic probes makes the size of the object under investigation irrelevant in terms of technique sensitivity. As a drawback, extensive site-directed mutagenesis is required in order to analyze the properties of the protein under investigation. EPR can provide detailed information on side chain dynamics of large membrane proteins or protein complexes embedded in membranes with an exquisite sensitivity for flexible regions and on water accessibility profiles across the membrane bilayer. Moreover, distances between the two spin-labeled side chains in membrane proteins can be detected with high precision at cryogenic temperatures. The application of EPR to membrane proteins still presents some challenges in terms of sample preparation, sensitivity and data interpretation, thus it is difficult to give ready-to-go methodological recipes. However, new technological developments (arbitrary waveform generators) and new spin labels spectroscopically orthogonal to nitroxides increased the range of applicability from in vitro toward in-cell EPR experiments. This chapter is an updated version of the one published in the first edition of the book and describes the state of the art in the application of nitroxide-based site-directed spin labeling EPR to membrane proteins, addressing new tools such as arbitrary waveform generators and spectroscopically orthogonal labels, such as Gd(III)-based labels. We will present challenges in sample preparation and data analysis for functional and structural membrane protein studies using site-directed spin labeling techniques and give experimental details on EPR techniques providing information on side chain dynamics and water accessibility using nitroxide probes. An updated optimal Q-band DEER setup for nitroxide probes will be described, and its extension to gadolinium-containing samples will be addressed.</p