Quantum Entanglement and Spin Control in Silicon Nanocrystal

Selective coherence control and electrically mediated exchange coupling of single electron spin between triplet and singlet states using numerically derived optimal control of proton pulses is demonstrated. We obtained spatial confinement below size of the Bohr radius for proton spin chain FWHM. Precise manipulation of individual spins and polarization of electron spin states are analyzed via proton induced emission and controlled population of energy shells in pure ²⁹Si nanocrystal. Entangled quantum states of channeled proton trajectories are mapped in transverse and angular phase space of ²⁹Si axial channel alignment in order to avoid transversal excitations. Proton density and proton energy as impact parameter functions are characterized in single particle density matrix via discretization of diagonal and nearest off-diagonal elements. We combined high field and low densities (1 MeV/92 nm) to create inseparable quantum state by superimposing the hyperpolarizationed proton spin chain with electron spin of ²⁹Si. Quantum discretization of density of states (DOS) was performed by the Monte Carlo simulation method using numerical solutions of proton equations of motion. Distribution of gaussian coherent states is obtained by continuous modulation of individual spin phase and amplitude. Obtained results allow precise engineering and faithful mapping of spin states. This would provide the effective quantum key distribution (QKD) and transmission of quantum information over remote distances between quantum memory centers for scalable quantum communication network. Furthermore, obtained results give insights in application of channeled protons subatomic microscopy as a complete versatile scanning-probe system capable of both quantum engineering of charged particle states and characterization of quantum states below diffraction limit linear and in-depth resolution.PACS numbers: 03.65.Ud, 03.67.Bg, 61.85.+p, 67.30.hj     

Mixed-time parallel evolution in multiple quantum NMR experiments: sensitivity and resolution enhancement in heteronuclear NMR

A new strategy is demonstrated that simultaneously enhances sensitivity and resolution in three- or higher-dimensional heteronuclear multiple quantum NMR experiments. The approach, referred to as mixed-time parallel evolution (MT-PARE), utilizes evolution of chemical shifts of the spins participating in the multiple quantum coherence in parallel, thereby reducing signal losses relative to sequential evolution. The signal in a given PARE dimension, t ₁, is of a non-decaying constant-time nature for a duration that depends on the length of t ₂, and vice versa, prior to the onset of conventional exponential decay. Line shape simulations for the ¹H–¹⁵N PARE indicate that this strategy significantly enhances both sensitivity and resolution in the indirect ¹H dimension, and that the unusual signal decay profile results in acceptable line shapes. Incorporation of the MT-PARE approach into a 3D HMQC-NOESY experiment for measurement of H^N–H^N NOEs in KcsA in SDS micelles at 50°C was found to increase the experimental sensitivity by a factor of 1.7±0.3 with a concomitant resolution increase in the indirectly detected ¹H dimension. The method is also demonstrated for a situation in which homonuclear ¹³C–¹³C decoupling is required while measuring weak H3′–2′OH NOEs in an RNA oligomer. Electronic Supplementary Material The online version of this article (doi:) contains supplementary material, which is available to authorized users.     

Extension of the HA-detection based approach: (HCA)CON(CA)H and (HCA)NCO(CA)H experiments for the main-chain assignment of intrinsically disordered proteins

Extensive resonance overlap exacerbates assignment of intrinsically disordered proteins (IDPs). This issue can be circumvented by utilizing ¹⁵N, ¹³C′ and ¹H^N spins, where the chemical shift dispersion is mainly dictated by the characteristics of consecutive amino acid residues. Especially ¹⁵N and ¹³C′ spins offer superior chemical shift dispersion in comparison to ¹³C^α and ¹³C^β spins. However, HN-detected experiments suffer from exchange broadening of amide proton signals on IDPs especially under alkali conditions. To that end, we propose here two novel HA-detected experiments, (HCA)CON(CA)H and (HCA)NCO(CA)H and a new assignment protocol based on panoply of unidirectional HA-detected experiments that enable robust backbone assignment of IDPs also at high pH. The new approach was tested at pH 6.5 and pH 8.5 on cancer/testis antigen CT16, a 110-residue IDP, and virtually complete backbone assignment of CT16 was obtained by employing the novel HA-detected experiments together with the previously introduced iH(CA)NCO scheme. Remarkably, also those 10 N-terminal residues that remained unassigned in our earlier HN-detection based assignment approach even at pH 6.5 were now readily assigned. Moreover, theoretical calculations and experimental results suggest that overall sensitivity of the new experiments is also applicable to small or medium sized globular proteins that require alkaline conditions.     

A novel strategy for the assignment of side-chain resonances in completely deuterated large proteins using 13C spectroscopy

The assignment of the aliphatic ¹³C resonances of trimeric Bacillus Subtilis chorismate mutase, a protein with a molecular mass of 44 kDa, consisting of three 127-residue monomers is presented by use of two-dimensional (2D) ¹³C-start and ¹³C-observe NMR experiments. These experiments start with ¹³C excitation and end with ¹³C observation while relying on the long transverse relaxation times of ¹³C spins in uniformly deuterated and ¹³C,¹⁵N-labeled large proteins. Gains in sensitivity are achieved by the use of a paramagnetic relaxation enhancement agent to reduce ¹³C T ₁ relaxation times with little effect on ¹³C T ₂ relaxation times. Such 2D ¹³C-only NMR experiments circumvent problems associated with the application of conventional experiments for side-chain assignment to proteins of larger sizes, for instance, the absence or low concentration of the side-chain ¹H spins, the transfer of the side-chain spin polarization to the ¹H^N spins for signal acquisition, or the necessity of a quantitative reprotonation of the methyl moieties in the otherwise fully deuterated side-chains. We demonstrate that having obtained a nearly complete assignment of the side-chain aliphatic ¹³C resonances, the side-chain ¹H chemical shifts can be assigned in a semiautomatic fashion using 3D ¹⁵N-resolved and ¹³C-resolved NOESY experiments measured with a randomly partially protonated protein sample. We also discuss perspectives for structure determination of larger proteins by using novel strategies which are based on the ¹H,¹H NOEs in combination with multiple residual dipolar couplings between adjacent ¹³C spins determined with 2D ¹³C-only experiments.     

A new horizon of DNP technology: application to in-vivo 13C magnetic resonance spectroscopy and imaging

Dynamic nuclear polarization (DNP) is an emerging technique for increasing the sensitivity (>10,000-fold) of magnetic resonance spectroscopy and imaging (MRSI), in particularly for low-γ nuclei. DNP methodology is based on polarizing nuclear spins in an amorphous solid state at low temperature (ca. 1 K) through coupling of the nuclear spins with unpaired electron spins that are added to the sample via an organic free radical. In an amorphous solid state, the high electron spin polarization can be transferred to the nuclear spins by microwave irradiation. While this technique has been utilized in solid-state research for many years, it is only recently that dissolution methods and the required hardware have been developed to produce the high nuclear polarization provided by DNP to produce injectable hyperpolarized solutions suitable for in vivo studies. It has been applied to a number of ¹³C-labeled cell metabolites in biological systems and their real-time metabolic conversion has been imaged. This review focuses briefly on the DNP methodology and the significant molecules investigated to date in preclinical cancer models, in terms of their downstream metabolism in vivo or the biological processes that they can probe. In particular, conversion between hyperpolarized ¹³C-labeled pyruvate and lactate, catalyzed by lactate dehydrogenase, has been shown to have a number of potential applications such as diagnosis, staging tumor grade, and monitoring therapy response. Strategies for making this technique more viable to use in clinical settings have been discussed.     

An estimate of spin diffusion in a spin subset: Application to iterative distance calculation from 3D 15N NOESY-HMQC

Summary A method for quantification of distances between amide hydrogens using only the 3D NOESY-HMQC experiment recorded on a ¹⁵N-labelled protein is presented. This method is based on an approximate expression of the NOE intensities between amide hydrogens obtained from continuum modelling of the non-amide spins; this expression is used in a distance calculation algorithm. The algorithm has been named CROWD, standing for Continuum approximation of Relaxati On path Ways between Dilute spins. This approximation as well as the CROWD algorithm are tested on a simulated case; the CROWD algorithm is then applied to experimental data, measured on a fragment of bacteriorhodopsin.     

Partially folded equilibrium intermediate of the villin headpiece HP67 defined by 13C relaxation dispersion

Identification and characterization of ensembles of intermediate states remains an important objective in describing protein folding in atomic detail. The 67-residue villin headpiece, HP67, consists of an N-terminal subdomain (residues 10–42) that transiently unfolds at equilibrium under native-like conditions and a highly stable C-terminal subdomain (residues 43–76). The transition between folded and unfolded states of the N-terminal domain has been characterized previously by ¹⁵N NMR relaxation dispersion measurements (Grey et al. in J Mol Biol 355:1078, 2006). In the present work, ¹³C spin relaxation was used to further characterize backbone and hydrophobic core contributions to the unfolding process. Relaxation of ¹³C^α spins was measured using the Hahn echo technique at five static magnetic fields (11.7, 14.1, 16.4, 18.8, and 21.1 T) and the Carr-Purcell-Meiboom-Gill (CPMG) relaxation dispersion method at a static magnetic field of 14.1 T. Relaxation of methyl ¹³C spins was measured using CPMG relaxation dispersion experiments at static magnetic fields of 14.1 and 18.8 T. Results for ¹³C and ¹⁵N spins yielded a consistent model in which the partially unfolded intermediate state of the N-terminal subdomain maintains residual structure for residues near the unprotonated His41 imidazole ring and in the interface between the N- and C-terminal subdomains. In addition, a second faster process was detected that appears to represent local dynamics within the folded state of the molecule and is largely confined to the hydrophobic interface between the N- and C-terminal subdomains.     

CO_H(N)CACB experiments for assigningbackbone resonances in 13C/15N-labeledproteins

A triple resonance NMR experiment, denoted CO_H(N)CACB, correlates¹H^N and ¹³CO spins with the¹³C and¹³C spins of adjacent amino acids. Thepulse sequence is an out-and-back design that starts with¹H^N magnetization and transfers coherence viathe ¹⁵N spin simultaneously to the ¹³CO and¹³C spins, followed by transfer to the¹³C spin. Two versions of the sequence arepresented: one in which the ¹³CO spins are frequency labeledduring an incremented t₁ evolution period prior to transfer ofmagnetization from the ¹³C to the¹³C resonances, and one in which the¹³CO spins are frequency labeled in a constant-time mannerduring the coherence transfer to and from the¹³C resonances. Because ¹³COand ¹⁵N chemical shifts are largely uncorrelated, thetechnique will be especially useful when degeneracy in the¹H^N-¹⁵N chemical shifts hindersresonance assignment. The CO_H(N)CACB experiment is demonstrated usinguniformly ¹³C/¹⁵N-labeled ubiquitin.     

Predicting Visual Consciousness Electrophysiologically from Intermittent Binocular Rivalry

Purpose

We sought brain activity that predicts visual consciousness.

Methods

We used electroencephalography (EEG) to measure brain activity to a 1000-ms display of sine-wave gratings, oriented vertically in one eye and horizontally in the other. This display yields binocular rivalry: irregular alternations in visual consciousness between the images viewed by the eyes. We replaced both gratings with 200 ms of darkness, the gap, before showing a second display of the same rival gratings for another 1000 ms. We followed this by a 1000-ms mask then a 2000-ms inter-trial interval (ITI). Eleven participants pressed keys after the second display in numerous trials to say whether the orientation of the visible grating changed from before to after the gap or not. Each participant also responded to numerous non-rivalry trials in which the gratings had identical orientations for the two eyes and for which the orientation of both either changed physically after the gap or did not.

Results

We found that greater activity from lateral occipital-parietal-temporal areas about 180 ms after initial onset of rival stimuli predicted a change in visual consciousness more than 1000 ms later, on re-presentation of the rival stimuli. We also found that less activity from parietal, central, and frontal electrodes about 400 ms after initial onset of rival stimuli predicted a change in visual consciousness about 800 ms later, on re-presentation of the rival stimuli. There was no such predictive activity when the change in visual consciousness occurred because the stimuli changed physically.

Conclusion

We found early EEG activity that predicted later visual consciousness. Predictive activity 180 ms after onset of the first display may reflect adaption of the neurons mediating visual consciousness in our displays. Predictive activity 400 ms after onset of the first display may reflect a less-reliable brain state mediating visual consciousness.     

Magnetic correlates in electromagnetic consciousness

ABSTRACT

We examine the hypothesis that consciousness is a manifestation of the electromagnetic field, finding supportive factors not previously considered. It is not likely that traditional electrophysiological signaling modes can be readily transmitted throughout the brain to properly enable this field because of electric field screening arising from the ubiquitous distribution of high dielectric lipid membranes, a problem that vanishes for low-frequency magnetic fields. Many reports over the last few decades have provided evidence that living tissue is robustly sensitive to ultrasmall (1–100 nT) ELF magnetic fields overlapping the γ-frequency range often associated with awareness. An example taken from animal behavior (coherent bird flocking) lends support to the possibility of a disembodied electromagnetic consciousness. In contrast to quantum consciousness hypotheses, the present approach is open to experimental trial.     

Out-and-back 13C–13C scalar transfers in protein resonance assignment by proton-detected solid-state NMR under ultra-fast MAS

We present here ¹H-detected triple-resonance H/N/C experiments that incorporate CO–CA and CA–CB out-and-back scalar-transfer blocks optimized for robust resonance assignment in biosolids under ultra-fast magic-angle spinning (MAS). The first experiment, (H)(CO)CA(CO)NH, yields ¹H-detected inter-residue correlations, in which we record the chemical shifts of the CA spins in the first indirect dimension while during the scalar-transfer delays the coherences are present only on the longer-lived CO spins. The second experiment, (H)(CA)CB(CA)NH, correlates the side-chain CB chemical shifts with the NH of the same residue. These high sensitivity experiments are demonstrated on both fully-protonated and 100 %-H^N back-protonated perdeuterated microcrystalline samples of Acinetobacter phage 205 (AP205) capsids at 60 kHz MAS.     

Photoaccumulation of the PsaB phyllosemiquinone in Photosystem I of Chlamydomonas reinhardtii

Photoaccumulation of membrane preparations of Chlamydomonas reinhardtii at pH 8 and 220 K reduces the primary and secondary electron acceptors in the Photosystem I (PSI) reaction centre, and produces a maximum of two spins per P700⁺. Proton electron nuclear double resonance (ENDOR) spectra demonstrate that the phyllosemiquinone produced is that attributed to the PsaA branch of electron transfer. Photoaccumulation at pH 10 and 220 K produces a maximum of four spins per P700⁺, and proton ENDOR spectra indicate that a second phyllosemiquinone is being photoaccumulated, with markedly different proton hyperfine couplings (hfcs). This phyllosemiquinone is unaffected by mutation of PsaAW693, confirming that it does not arise from the PsaA branch of electron transfer, and we therefore attribute it to the PsaB phyllosemiquinone.     

CRITICAL IRRADIANCE LEVELS AND THE INTERACTIVE EFFECTS OF QUANTUM IRRADIANCE AND DOSE ON GAMETOGENESIS IN THE GIANT KELP,MACROCYSTIS PYRIFERA1

Gametophytes of Macrocystis pyrifera (L.) C. Ag. were cultured under a series of quantum irradiances in three photoperiod regimes. The quantum irradiances in each photoperiod were adjusted to provide equal daily irradiation dosages between photoperiods which allowed a critical examination of the interactions between quantum irradiance and quantum dose in determining gametophyte fertility. The lowest quantum irradiance which stimulated gametogenesis in more than 50% of the female gametophytes was 5 μE·m^?2·s^?1. The saturating irradiance was ca. 10 μE·m^?2·s^?1 at photoperiods of 12 h or greater. In terms of daily quantum dose, the lowest dose at which greater than 50% gametogenesis occurred was 0.2 E·m^?2·d^?1. However, this critical quantum dose was higher (0.4 E·m^?2·d^?1) when instantaneous irradiances were less than 5 μE·m^?2·s^?1. The saturation quantum dose was also affected by the rate at which the quantum dose was received and varied from 0.4 to 0.8 E·m^?2·d^?1. Gametophytes in all three photoperiods reached 100% fertility at quantum irradiances above 5 μE·m^?2·s^?1. Photoperiod effects were small and could be accounted for by quantum dosage effects.     

Quantum computing with molecular magnets

We discuss the potential of molecular magnets as the building blocks of a quantum computer. The simplification in the control procedure for the quantum gates in many-spin systems coming from the high symmetry is shown to lead to a relatively simple way to address the spin degrees of freedom in molecular magnets. The advantage of an anisotropic effective spin interaction in memory applications is demonstrated on the example of the Grover quantum search algorithm in a generic easy-axis molecular magnet. Electric control of the coupling between the spins is shown to enable two-qubit quantum gates in polyoxometalates.     

The use of TROSY for detection and suppression of conformational exchange NMR line broadening in biological macromolecules

The interference between conformational exchange-induced time-dependent variations of chemical shifts in a pair of scalar coupled ¹H and ¹⁵N spins is used to construct novel TROSY-type NMR experiments to suppress NMR signal loss in [¹⁵N,¹H]-correlation spectra of a 14-mer DNA duplex free in solution and complexed with the Antp homeodomain. An analysis of double- and zero-quantum relaxation rates of base ¹H–¹⁵N moieties showed that for certain residues the contribution of conformational exchange-induced transverse relaxation might represent a dominant relaxation mechanism, which, in turn, can be effectively suppressed by TROSY. The use of the new TROSY method for exchange-induced transverse relaxation optimization is illustrated with two new experiments, 2D ^h1 J _HN,^h2 J _NN-quantitative [¹⁵N,¹H]-TROSY to measure ^h1 J _HN and ^h2 J _NN scalar coupling constants across hydrogen bonds in nucleic acids, and 2D (^h2 J _NN+^h1 J _NH)-correlation-[¹⁵N,¹H]-TROSY to correlate ¹H^N chemical shifts of bases with the chemical shifts of the tertiary ¹⁵N spins across hydrogen bonds using the sum of the trans-hydrogen bond coupling constants in nucleic acids.     

An investigation into possible quantum chaos in the H<Subscript>2</Subscript> molecule under intense laser fields via Ehrenfest phase space (EPS) trajectories

By employing the Ehrenfest "phase space" trajectory method for studying quantum chaos, developed in our laboratory, the present study reveals that the H₂ molecule under intense laser fields of three different intensities, I?=?1?×?10¹⁴ W/cm², 5?×?10¹⁴ W/cm², and 1?×?10¹⁵ W/cm², does not show quantum chaos. A similar conclusion is also reached through the Loschmidt echo (also called quantum fidelity) calculations reported here for the first time for a real molecule under intense laser fields. Thus, a long-standing conjecture about the possible existence of quantum chaos in atoms and molecules under intense laser fields has finally been tested and not found to be valid in the present case.     

Extending the range of amide proton relaxation dispersion experiments in proteins using a constant-time relaxation-compensated CPMG approach

Relaxation compensated constant-time Carr–Purcell–Meiboom–Gill relaxation dispersion experiments for amide protons are presented that detect s-ms time-scale dynamics of protein backbone amide sites. Because of their ten-fold larger magnetogyric ratio, much shorter 180° pulses can be applied to ¹H than to ¹⁵N spins; therefore, off-resonance effects are reduced and a wider range of effective rf fields can often be used in the case of ¹H experiments. Applications to [¹H-¹⁵N]-ubiquitin and [¹H-¹⁵N]-perdeuterated HIV-1 protease are discussed. In the case of ubiquitin, we present a pulse sequence that reduces artifacts that arise from homonuclear ³J(H_N-H) coupling. In the case of the protease, we show that relaxation dispersion of both ¹H and ¹⁵N spins provides a more comprehensive picture of slow backbone dynamics than does the relaxation dispersion of either spin alone. We also compare the relative merits of ¹H versus ¹⁵N transverse relaxation measurements and note the benefits of using a perdeuterated protein to measure the relaxation dispersion of both spin types.     

BEST and SOFAST experiments for resonance assignment of histidine and tyrosine side chains in <Superscript>13</Superscript>C/<Superscript>15</Superscript>N labeled proteins

Aromatic amino-acid side chains are essential components for the structure and function of proteins. We present herein a set of NMR experiments for time-efficient resonance assignment of histidine and tyrosine side chains in uniformly ¹³C/¹⁵N-labeled proteins. The use of band-selective ¹³C pulses allows to deal with linear chains of coupled spins, thus avoiding signal loss that occurs in branched spin systems during coherence transfer. Furthermore, our pulse schemes make use of longitudinal ¹H relaxation enhancement, Ernst-angle excitation, and simultaneous detection of ¹H and ¹³C steady-state polarization to achieve significant signal enhancements.