Research ArticleQUANTUM INFORMATION

A molecular quantum spin network controlled by a single qubit

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Science Advances  11 Aug 2017:
Vol. 3, no. 8, e1701116
DOI: 10.1126/sciadv.1701116
  • Fig. 1 Spectroscopy of few spin-labeled peptides.

    Electron spin spectra measured at T = 4.2 K and ultrahigh vacuum (UHV); (A) Experimental sketch: The shallow NV center spin couples to doubly spin-labeled polyprolines. Coherent control over all participating spins is provided by a close-by (~ 50 μm) microwave wire (MW). The edge of the depicted sphere is the maximum sensing radius for a single electron spin to be detected, delimited by the NV centers’ T2 time. The intrapeptide coupling is almost two orders of magnitude larger than any of the other couplings in the few-peptide case, especially the interpeptide coupling. (B) Pulse sequence used to probe the spectrum of external network spins. Red pulses address the NV center spin, whereas the frequency of the blue pulse is swept to address network spin labels (SL). (C) Measured spectrum on a diamond membrane coated exclusively with spin-labeled peptides. The fit of the spectrum is a numerical simulation over random orientations of 50 MTSSL spin labels, including decoherence effects due to interpeptide couplings. a.u., arbitrary units. (D) Same as (C) but the labeled polyprolines were diluted with unlabeled ones at a ratio of 1:10. Distinct hyperfine couplings are clearly visible. (E) Measurement of a diamond dangling bond dark spin on a cleaned membrane for comparison.

  • Fig. 2 Coupling to only few MTSSL spin-labels.

    (A) Coherent oscillation due to dipolar couplings between sensor and network spins, clearly visible by contrast inversion (blue shaded area) of the NV probe spin state, which suggests a low number of participating network spins. For the measurement, we choose a constant evolution time of 19.8 μs for the NV probe spin Hahn echo sequence, maximizing interaction time. Previous to the measurement, T2 = 14.0 μs of the NV center under investigation was measured. To access the coupling between sensor and network spins, we sweep the application point of the network π pulse within the free evolution of the sensor spin coherence. The measurement data are accompanied by simulations of coupling strength oscillations caused by n = 2, 6, and 10 randomly distributed spins above the diamond surface. We would like to stress that it is difficult to estimate the precise number of spins here, and the relative strength of the overshoot below the NV sensor mixed state (0.5) heavily depends on the couplings (positions) of the participating network spins. (B) Hahn echo measurement on the external network spins directly probing their T2 time via the readable signal from the probe spin (red). The blue curve was measured on a pulsed EPR spectrometer at 10 K in a frozen solution of water/glycerol (4:1) using the same peptides. A low concentration guarantees a proper separation between peptides, and the agreement of both coherence times points toward comparable SDSL peptide-peptide distances in both samples.

  • Fig. 3 Access to dipolar coupling between MTSSL spins.

    (A) Measurement of a triple-resonance frequency sweep on a few network spins (Figs. 1D and 2) with a π pulse width of 3.4 MHz. The swept frequency channel is SL 2, whereas SL 1 is kept at zero detuning to create a coherent superposition. The resulting spectrum can be fitted with two Lorentzians (red), as is expected from a pronounced J coupling between network spins. (B) Delay measurement on a the same environment, where we fix the excitation frequency of SL 1 at the network Larmor frequency and the SL 2 sweeping π pulse frequency 3 MHz apart from it. The red curve is a fit using a decaying cosine. The oscillations reveal the very same coupling strength as the frequency sweep in (A).

  • Fig. 4 Schemes for spin network applications.

    (A) Schematic representation of the envisaged probe–controlled spin network (with intracell and intercell couplings, J and J′, respectively), equipped with an atomic force microscopy magnetic tip to generate gradient fields on nanometer length scales. (B) Extension of the multi-electron spectroscopy to extract intercell couplings, which can further lead to the structural analysis of the spin network. By varying the π pulse time on the second τ, we arrive at the Fourier components of the observed probe spin response. (C) Remote communication between two probes via a spin chain is shown, where the response on the probe spin B, Embedded Image, varies by sweeping the frequency of the probe A. When ωA = ωB, the quantum state of probe A is transferred to B. (D) The effect of the quantum critical point (QCP) in a transverse Ising chain on the state transfer between the two remote probes. At QCP corresponding to ω = J, the fidelity drastically increases—indicating enhanced long-range correlations in the chain.

Supplementary Materials

  • Supplementary material for this article is available at http://advances.sciencemag.org/cgi/content/full/3/8/e1701116/DC1

    section S1. Model Hamiltonian

    section S2. Modeling of pulse sequences

    section S3. Controlling the spin network

    section S4. Matrix-assisted laser desorption/ionization (MALDI)

    section S5. EPR spectroscopy

    section S6. Measurements under ambient conditions

    fig. S1. Simulation of the Hamiltonian under DEER spectroscopy.

    fig. S2. Simulation of the Hamiltonian under triple electron-electron resonance (TEER) spectroscopy.

    fig. S3. MALDI measurement.

    fig. S4. Continuous wave (CW) and pulsed EPR measurements.

    fig. S5. DEER spectroscopy under ambient conditions.

    References (4649)

  • Supplementary Materials

    This PDF file includes:

    • section S1. Model Hamiltonian
    • section S2. Modeling of pulse sequences
    • section S3. Controlling the spin network
    • section S4. Matrix-assisted laser desorption/ionization (MALDI)
    • section S5. EPR spectroscopy
    • section S6. Measurements under ambient conditions
    • fig. S1. Simulation of the Hamiltonian under DEER spectroscopy.
    • fig. S2. Simulation of the Hamiltonian under triple electron-electron resonance
      (TEER) spectroscopy.
    • fig. S3. MALDI measurement.
    • fig. S4. Continuous wave (CW) and pulsed EPR measurements.
    • fig. S5. DEER spectroscopy under ambient conditions.
    • References (46–49)

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