Differential privacy provides a rigorous standard for evaluating the privacy of perturbation algorithms. It has widely been regarded that differential privacy is a universal definition that deals with both independent and correlated data and a differentially private algorithm can protect privacy against arbitrary adversaries. However, recent research indicates that differential privacy may not guarantee privacy against arbitrary adversaries if the data are correlated.In this paper, we focus on the private perturbation algorithms on correlated data. We investigate the following three problems: (1) the influence of data correlations on privacy;(2) the influence of adversary prior knowledge on privacy; and (3) a general perturbation algorithm that is private for prior knowledge of any subset of tuples in the data when the data are correlated. We propose a Pufferfish definition of privacy, called Bayesian differential privacy, by which the privacy level of a probabilistic perturbation algorithm can be evaluated even when the data are correlated and when the prior knowledge is incomplete. We present a Gaussian correlation model to accurately describe the structure of data correlations and analyze the Bayesian differential privacy of the perturbation algorithm on the basis of this model. Our results show that privacy is poorest for an adversary who has the least prior knowledge. We further extend this model to a more general one that considers uncertain prior knowledge.
Cross polarization/magic angle spinning (CP/MAS)(13)C (solid state high resolution) NMR spectra were observed for chlorosomes and BChlc aggregates. Similarity of both kinds of spectra (except for some signals assignable to proteins and lipids in chlorosomes) indicates that BChlc's in chlorosomes are present just as in synthetic BChlc aggregates. Chemical shifts for C13(1) carbonyl and C3(1) hydroxylethyl carbons indicate hydrogen bonding between them. Comparison of solution and solid state(13)C NMR chemical shifts shows the five coordinated nature of BChlc aggregates. Some chemical shift differences were attributable to ring currents shifts. Their comparisons with calculated ring current shift values predicted structures for the aggregates. Cross polarization dynamics of the CP/MAS(13)C NMR signals explored dynamic and structural nature of the BChlc aggregates.
Development of quality estimation models using near infrared spectroscopy (NIRS) and multivariate analysis has been accelerated as a process analytical technology (PAT) tool in the pharmaceutical industry. Although linear regression methods such as partial least squares (PLS) are widely used, they cannot always achieve high estimation accuracy because physical and chemical properties of a measuring object have a complex effect on NIR spectra. In this research, locally weighted PLS (LW-PLS) which utilizes a newly defined similarity between samples is proposed to estimate active pharmaceutical ingredient (API) content in granules for tableting. In addition, a statistical wavelength selection method which quantifies the effect of API content and other factors on NIR spectra is proposed. LW-PLS and the proposed wavelength selection method were applied to real process data provided by Daiichi Sankyo Co., Ltd., and the estimation accuracy was improved by 38.6% in root mean square error of prediction (RMSEP) compared to the conventional PLS using wavelengths selected on the basis of variable importance on the projection (VIP). The results clearly show that the proposed calibration modeling technique is useful for API content estimation and is superior to the conventional one.
To understand the effect of hydration on protein dynamics, inelastic neutron-scattering experiments were performed on staphylococcal nuclease samples at differing hydration levels: dehydrated, partially hydrated, and hydrated. At cryogenic temperatures, hydration affected the collective motions with energies lower than 5 meV, whereas the high-energy localized motions were independent of hydration. The prominent change was a shift of boson peak toward higher energy by hydration, suggesting a hardening of harmonic potential at local minima on the energy landscape. The 240 K transition was observed only for the hydrated protein. Significant quasielastic scattering at 300 K was observed only for the hydrated sample, indicating that the origin of the transition is the motion activated by hydration water. The neutron-scattering profile of the partially hydrated sample was quite similar to that of the hydrated sample at 100 K and 200 K, whereas it was close to the dehydrated sample at 300 K, indicating that partial hydration is sufficient to affect the harmonic nature of protein dynamics, and that there is a threshold hydration level to activate anharmonic motions. Thus, hydration water controls both harmonic and anharmonic protein dynamics by differing means.
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