Publications by authors named "Kestner J"

In this paper, we numerically optimize broadband pulse shapes that maximize Hahn echo amplitudes. Pulses are parameterized as neural networks (NN), nonlinear amplitude limited Fourier series (FS), and discrete time series (DT). These are compared to an optimized choice of the conventional hyperbolic secant (HS) pulse shape.

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In semiconductor spin qubits which typically interact through short-range exchange coupling, shuttling of spin is a practical way to generate quantum operations between distant qubits. Although the exchange is often tunable through voltages applied to gate electrodes, its minimal value can be significantly large, which hinders the applicability of existing shuttling protocols to such devices, requiring a different approach. In this work, we extend our previous results for double- and triple-dot systems, and describe a method for implementing spin state transfer in long chains of singly occupied quantum dots in a non-adiabatic manner.

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We derive a set of composite pulse sequences that generates cnot gates and correct all systematic errors within the logical subspace to arbitrary order. These sequences are applicable for any two-qubit interaction Hamiltonian and make no assumptions about the underlying noise mechanism except that it is constant on the time scale of the operation. We do assume access to high-fidelity single-qubit gates, so single-qubit gate imperfections eventually limit the achievable fidelity.

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We develop a systematic method of performing corrected gate operations on an array of exchange-coupled singlet-triplet qubits in the presence of both fluctuating nuclear Overhauser field gradients and charge noise. The single-qubit control sequences we present have a simple form, are relatively short, and form the building blocks of a corrected cnot gate when also implemented on the interqubit exchange link. This is a key step towards enabling large-scale quantum computation in a semiconductor-based architecture by facilitating error reduction below the quantum error correction threshold for both single-qubit and multiqubit gate operations.

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Precise qubit manipulation is fundamental to quantum computing, yet experimental systems generally have stray coupling between the qubit and the environment, which hinders the necessary high-precision control. Here, we report the first theoretical progress in correcting an important class of errors stemming from fluctuations in the magnetic field gradient, in the context of the singlet-triplet spin qubit in a semiconductor double quantum dot. These errors are not amenable to correction via control techniques developed in other contexts, as here the experimenter has precise control only over the rotation rate about the z axis of the Bloch sphere, and this rate is furthermore restricted to be positive and bounded.

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Introduction: The unique electromagnetic environment of the magnetic resonance imaging (MRI) scanner presents particular problems for critically ill patients requiring mechanical ventilation during MRI. Most currently available MRI-compatible ventilators are limited in scope and function and thus may not be suitable for patients requiring high peak inspiratory pressure or flow.

Methods: To determine whether a standard critical care ventilator could be used under MRI conditions, we modified a Siemens Servo 900C by replacing the standard oxygen blender with an MRI-compatible blender.

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Objective: To determine the pharmacologic activity of over-the-counter (OTC) thyroid preparations.

Design: In vitro analysis and a prospective, crossover study in vivo.

Setting: Tertiary care center.

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We applied stepwise regression for multivariate analysis of data for free thyroxin (FT4) in serum and for other laboratory tests of thyroid function in patients with nonthyroidal illness. Using the maximum R2 improvement and backward elimination methods to test five variables [prealbumin, albumin, T4-binding globulin (TBG), free fatty acids (FFA), and FFA/albumin molar ratio], we found that the variables with the greatest predictive power clustered according to the methodology of FT4 measurement. Thus, we best predicted the FT4 results obtained by 16 techniques as follows: FT4 measured by one-step (analog) RIAs, with albumin; FT4 determined by two-step (sequential) RIAs, with FFA or FFA/albumin molar ratio; FT4 estimated by a binding-rate-based RIA or conceptually related FT4 indices [based on triiodothyronine (T3) uptake], with TBG; FT4 measured by equilibrium dialysis, with TBG and FFA/albumin molar ratio; and T4/TBG ratios, with either none or prealbumin and albumin.

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We studied the correlation of thyroxin (T4)-binding proteins with the apparent free T4 (FT4) in 101 patients with nonthyroidal illness (NTI). Most patients (95%) were seriously ill at the time of blood collection. Concentrations of T4-binding prealbumin (transthyretin), albumin, and T4-binding globulin (TBG) often were low in the sera of these patients.

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We examined the effect of endogenous free fatty acids (FFA) on the measurement of free thyroxin (FT4) by five different methodologies represented in 16 different assays in a large number of patients with nonthyroidal illness (NTI). Some, but not all, one-step (analog) FT4 RIAs negatively correlated with FFA concentration. All two-step FT4 RIAs, equilibrium dialysis FT4, and the dialyzable (free) fraction of T4 positively correlated.

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The authors compared results for accuracy and precision obtained by a semiautomated prototype International Remote Imaging Systems, Inc. (IRIS) urinalysis workstation (IUW) with those from quantitative manual urinalysis (QMU). Three technologists skilled in urinalysis each performed 172 urinalyses with both the IUW and QMU methods.

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The rate of the Jaffé reaction depends on the concentration of sodium hydroxide; the pseudo-first-order rate constant of the reaction, at 37 degrees C in 10 mmol/L picrate solution, is 0.004 mmol/L. We formulated an automated method to determine urinary creatinine directly without manual sample dilution.

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The proportional bias of four methods frequently used for determining low concentrations of protein was evaluated with human serum protein fractions (Cohn Fractions II, III, IV, and V). Each fraction was assigned a protein concentration value as determined by the biuret method, calibrated with purified human serum albumin monomer. All four methods (Coomassie Brilliant Blue dye-binding, the method of Lowry et al.

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