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Quantum memories capable of storing and retrieving coherent information for extended times at room temperature would enable a host of new technologies. Electron and nuclear spin qubits using shallow neutral donors in semiconductors have been studied extensively but are limited to low temperatures (<̰10 kelvin); however, the nuclear spins of ionized donors have the potential for high-temperature operation. We used optical methods and dynamical decoupling to realize this potential for an ensemble of phosphorous-31 donors in isotopically purified silicon-28 and observed a room-temperature coherence time of over 39 minutes. We further showed that a coherent spin superposition can be cycled from 4.2 kelvin to room temperature and back, and we report a cryogenic coherence time of 3 hours in the same system.

Quantum memories capable of storing and retrieving coherent information for extended times at room temperature would enable a host of new technologies. Electron and nuclear spin qubits using shallow neutral donors in semiconductors have been studied extensively but are limited to low temperatures (\\(\\)10 K); however, the nuclear spins of ionized donors have potential for high temperature operation. We use optical methods and dynamical decoupling to realize this potential for an ensemble of 31P donors in isotopically purified 28Si and observe a room temperature coherence time of over 39 minutes. We further show that a coherent spin superposition can be cycled from 4.2 K to room temperature and back, and report a cryogenic coherence time of 3 hours in the same system.

We revisit the analysis of sharp infinite potentials within the path integral formalism using the image method [1]. We show that the use of a complete set of energy eigenstates that satisfy the boundary conditions of an infinite wall precisely generates the propagator proposed in Ref. [1]. We then show the validity of the image method by using supersymmetric quantum mechanics to relate a potential without a sharp boundary to the infinite square well and derive its propagator with an infinite number of image charges. Finally, we show that the image method readily generates the propagator for the half-harmonic oscillator, a potential that has a sharp infinite boundary at the origin and a quadratic potential in the allowed region, and leads to the well known eigenvalues and eigenfunctions.

Donor spins in silicon are some of the most promising qubits for upcoming solid-state quantum technologies. The nuclear spins of phosphorus donors in enriched silicon have among the longest coherence times of any solid-state system as well as simultaneous qubit initialization, manipulation and readout fidelities near ~99.9%. Here we characterize the phosphorus in silicon system in the regime of \"zero\" magnetic field, where a singlet-triplet spin clock transition can be accessed, using laser spectroscopy and magnetic resonance methods. We show the system can be optically hyperpolarized and has ~10 s Hahn echo coherence times, even at Earth's magnetic field and below.

We have applied two-dimensional infrared (2D IR) and βν correlation spectroscopy to in-situ IR spectroscopy of pulmonary surfactant proteins SP-B and SP-C in lipid–protein monolayers at the air—water interface. For both SP-B and SP-C, a statistical windowed autocorrelation method identified two separate surface pressure regions that contained maximum amide I intensity changes: 4–25 mN/m and 25–40 mN/m. For SP-C, 2D IR and βν correlation analyses of these regions indicated that SP-C adopts a variety of secondary structure conformations, including α-helix, β-sheet, and an intermolecular aggregation of extended β-sheet structure. The main α-helix band split into two peaks at high surface pressures, indicative of two different helix conformations. At low surface pressures, all conformations of the SP-C molecule reacted identically to increasing surface pressure and reoriented in phase with each other. Above 25 mN/m, however, the increasing surface pressure selectively affected the coexisting protein conformations, leading to an independent reorientation of the protein conformations. The asynchronous 2D IR spectrum of SP-B showed the presence of two α-helix components, consistent with two separate populations of α-helix in SP-B—a hydrophobic fraction associated with the lipid chains and a hydrophilic fraction parallel to the membrane surface. The distribution of correlation intensity between the two α-helix cross peaks indicated that the more hydrophobic helix fraction predominates at low surface pressures whereas the more hydrophilic helix fraction predominates at high surface pressures. The different SP-B secondary structures reacted identically to increasing surface pressure, leading to a reorientation of all SP-B subunits in phase with one another.

We have applied two-dimensional infrared (2D IR) and beta(nu) correlation spectroscopy to in-situ IR spectroscopy of pulmonary surfactant proteins SP-B and SP-C in lipid-protein monolayers at the air--water interface. For both SP-B and SP-C, a statistical windowed autocorrelation method identified two separate surface pressure regions that contained maximum amide I intensity changes: 4-25 mN/m and 25-40 mN/m. For SP-C, 2D IR and beta(nu) correlation analyses of these regions indicated that SP-C adopts a variety of secondary structure conformations, including alpha-helix, beta-sheet, and an intermolecular aggregation of extended beta-sheet structure. The main alpha-helix band split into two peaks at high surface pressures, indicative of two different helix conformations. At low surface pressures, all conformations of the SP-C molecule reacted identically to increasing surface pressure and reoriented in phase with each other. Above 25 mN/m, however, the increasing surface pressure selectively affected the coexisting protein conformations, leading to an independent reorientation of the protein conformations. The asynchronous 2D IR spectrum of SP-B showed the presence of two alpha-helix components, consistent with two separate populations of alpha-helix in SP-B--a hydrophobic fraction associated with the lipid chains and a hydrophilic fraction parallel to the membrane surface. The distribution of correlation intensity between the two alpha-helix cross peaks indicated that the more hydrophobic helix fraction predominates at low surface pressures whereas the more hydrophilic helix fraction predominates at high surface pressures. The different SP-B secondary structures reacted identically to increasing surface pressure, leading to a reorientation of all SP-B subunits in phase with one another.

We have applied two-dimensional infrared (2D IR) and betanu correlation spectroscopy to in-situ IR spectroscopy of pulmonary surfactant proteins SP-B and SP-C in lipid-protein monolayers at the air-water interface. For both SP-B and SP-C, a statistical windowed autocorrelation method identified two separate surface pressure regions that contained maximum amide I intensity changes: 4-25 mN/m and 25-40 mN/m. For SP-C, 2D IR and betanu correlation analyses of these regions indicated that SP-C adopts a variety of secondary structure conformations, including alpha-helix, beta-sheet, and an intermolecular aggregation of extended beta-sheet structure. The main alpha-helix band split into two peaks at high surface pressures, indicative of two different helix conformations. At low surface pressures, all conformations of the SP-C molecule reacted identically to increasing surface pressure and reoriented in phase with each other. Above 25 mN/m, however, the increasing surface pressure selectively affected the coexisting protein conformations, leading to an independent reorientation of the protein conformations. The asynchronous 2D IR spectrum of SP-B showed the presence of two alpha-helix components, consistent with two separate populations of alpha-helix in SP-B-a hydrophobic fraction associated with the lipid chains and a hydrophilic fraction parallel to the membrane surface. The distribution of correlation intensity between the two alpha-helix cross peaks indicated that the more hydrophobic helix fraction predominates at low surface pressures whereas the more hydrophilic helix fraction predominates at high surface pressures. The different SP-B secondary structures reacted identically to increasing surface pressure, leading to a reorientation of all SP-B subunits in phase with one another.