Structure stability and carrier localization inCdX(X=S,Se,Te)semiconductors

2000 ◽  
Vol 62 (11) ◽  
pp. 6944-6947 ◽  
Author(s):  
Su-Huai Wei ◽  
S. B. Zhang
Keyword(s):  
Structure Stability ◽  
Carrier Localization

Development and Psychometric Evaluation of a Revised Sense of Coherence Scale

2018 ◽  
Vol 34 (3) ◽  
pp. 206-215 ◽  
Author(s):  
Rahel Bachem ◽  
Andreas Maercker
Keyword(s):  
Posttraumatic Growth ◽  
Factor Structure ◽  
Sense Of Coherence ◽  
Psychological Health ◽  
Psychometric Evaluation ◽  
Health Indicators ◽  
Structure Stability ◽  
Confirmatory Factor Analyses ◽  
Reliability Factor ◽  
Two Samples

Abstract. The present study introduces a revised Sense of Coherence (SOC) scale, a new conceptualization and operationalization of the resilience indicator SOC. It outlines the scale development and aims for testing its reliability, factor structure, and validity. Literature on Antonovsky’s SOC (SOC-A) was critically reviewed to identify needs for improving the scale. The scale was investigated in two samples. Sample 1 consisted of 334 bereaved participants, Sample 2 of 157 healthy controls. The revised SOC Scale, SOC-A, and theoretically relevant questionnaires were applied. Explorative and confirmatory factor analyses established a three-factor structure in both samples. The revised SOC Scale showed significant but discriminative associations with related constructs, including self-efficacy, posttraumatic growth, and neuroticism. The revised measure was significantly associated with psychological health indicators, including persistent grief, depression, and anxiety, but not to the extent as the previous SOC-A. Stability over time was sufficient. The study provides psychometric support for the revised SOC conceptualization and scale. It has several advantages over the previous SOC-A scale (unique variance, distinct factor structure, stability). The scale could be used for clinical and health psychological testing or research into the growing field of studies on resilience over the life span.

Structure, Stability and Water Adsorption on Ultra-Thin TiO2 Supported on TiN

2019 ◽  
Author(s):  
Jose Julio Gutierrez Moreno ◽  
Marco Fronzi ◽  
Pierre Lovera ◽  
alan O'Riordan ◽  
Mike J Ford ◽  
...  
Keyword(s):  
Density Functional ◽  
Water Adsorption ◽  
Chemical Potential ◽  
Energy Gap ◽  
Molecular Water ◽  
Structure Stability ◽  
Ambient Conditions ◽  
Rutile Structure ◽  
The Stability ◽  
The One

<p></p><p>Interfacial metal-oxide systems with ultrathin oxide layers are of high interest for their use in catalysis. In this study, we present a density functional theory (DFT) investigation of the structure of ultrathin rutile layers (one and two TiO<sub>2</sub> layers) supported on TiN and the stability of water on these interfacial structures. The rutile layers are stabilized on the TiN surface through the formation of interfacial Ti–O bonds. Charge transfer from the TiN substrate leads to the formation of reduced Ti<sup>3+</sup> cations in TiO<sub>2.</sub> The structure of the one-layer oxide slab is strongly distorted at the interface, while the thicker TiO<sub>2</sub> layer preserves the rutile structure. The energy cost for the formation of a single O vacancy in the one-layer oxide slab is only 0.5 eV with respect to the ideal interface. For the two-layer oxide slab, the introduction of several vacancies in an already non-stoichiometric system becomes progressively more favourable, which indicates the stability of the highly non-stoichiometric interfaces. Isolated water molecules dissociate when adsorbed at the TiO<sub>2</sub> layers. At higher coverages the preference is for molecular water adsorption. Our ab initio thermodynamics calculations show the fully water covered stoichiometric models as the most stable structure at typical ambient conditions. Interfacial models with multiple vacancies are most stable at low (reducing) oxygen chemical potential values. A water monolayer adsorbs dissociatively on the highly distorted 2-layer TiO<sub>1.75</sub>-TiN interface, where the Ti<sup>3+</sup> states lying above the top of the valence band contribute to a significant reduction of the energy gap compared to the stoichiometric TiO<sub>2</sub>-TiN model. Our results provide a guide for the design of novel interfacial systems containing ultrathin TiO<sub>2</sub> with potential application as photocatalytic water splitting devices.</p><p></p>

pH-Dependent Thermal Stability of Vibrio cholerae L-asparaginase

2019 ◽  
Vol 26 (10) ◽  
pp. 743-750 ◽  
Author(s):  
Remya Radha ◽  
Sathyanarayana N. Gummadi
Keyword(s):  
Vibrio Cholerae ◽  
Conformational Changes ◽  
Kinetic Studies ◽  
Structural Features ◽  
Structure Stability ◽  
Kcal Mole ◽  
Scanning Calorimetry ◽  
Wide Range ◽  
Ph Dependent ◽  
Ph Range

Background:pH is one of the decisive macromolecular properties of proteins that significantly affects enzyme structure, stability and reaction rate. Change in pH may protonate or deprotonate the side group of aminoacid residues in the protein, thereby resulting in changes in chemical and structural features. Hence studies on the kinetics of enzyme deactivation by pH are important for assessing the bio-functionality of industrial enzymes. L-asparaginase is one such important enzyme that has potent applications in cancer therapy and food industry.Objective:The objective of the study is to understand and analyze the influence of pH on deactivation and stability of Vibrio cholerae L-asparaginase.Methods:Kinetic studies were conducted to analyze the effect of pH on stability and deactivation of Vibrio cholerae L-asparaginase. Circular Dichroism (CD) and Differential Scanning Calorimetry (DSC) studies have been carried out to understand the pH-dependent conformational changes in the secondary structure of V. cholerae L-asparaginase.Results:The enzyme was found to be least stable at extreme acidic conditions (pH< 4.5) and exhibited a gradual increase in melting temperature from 40 to 81 °C within pH range of 4.0 to 7.0. Thermodynamic properties of protein were estimated and at pH 7.0 the protein exhibited ΔG37of 26.31 kcal mole-1, ΔH of 204.27 kcal mole-1 and ΔS of 574.06 cal mole-1 K-1.Conclusion:The stability and thermodynamic analysis revealed that V. cholerae L-asparaginase was highly stable over a wide range of pH, with the highest stability in the pH range of 5.0–7.0.

Structure, stability, and vibrational properties of polymerizedC60

1995 ◽  
Vol 52 (20) ◽  
pp. 14963-14970 ◽  
Author(s):  
Dirk Porezag ◽  
Mark R. Pederson ◽  
Th. Frauenheim ◽  
Th. Köhler
Keyword(s):  
Structure Stability ◽  
Vibrational Properties

Enabling highly structure stability and adsorption performances of Li1.6Mn1.6O4 by Al-gradient surface doping

2021 ◽  
Vol 264 ◽  
pp. 118433
Author(s):  
Fangren Qian ◽  
Min Guo ◽  
Zhiqiang Qian ◽  
Bing Zhao ◽  
Jun Li ◽  
...  
Keyword(s):  
Structure Stability ◽  
Surface Doping ◽  
Gradient Surface

scholarly journals Combined Method to Remove Endotoxins from Protein Nanocages for Drug Delivery Applications: The Case of Human Ferritin

Pharmaceutics ◽  
2021 ◽  
Vol 13 (2) ◽  
pp. 229
Author(s):  
Filippo Silva ◽  
Leopoldo Sitia ◽  
Raffaele Allevi ◽  
Arianna Bonizzi ◽  
Marta Sevieri ◽  
...  
Keyword(s):  
Drug Delivery ◽  
Biological Fluids ◽  
Affinity Purification ◽  
Delivery Systems ◽  
Point Of View ◽  
Uniform Structure ◽  
Structure Stability ◽  
Target Cells ◽  
Clinical Phase ◽  
Main Challenge

Protein nanocages represent an emerging candidate among nanoscaled delivery systems. Indeed, they display unique features that proved to be very interesting from the nanotechnological point of view such as uniform structure, stability in biological fluids, suitability for surface modification to insert targeting moieties and loading with different drugs and dyes. However, one of the main concerns regards the production as recombinant proteins in E. coli, which leads to a product with high endotoxin contamination, resulting in nanocage immunogenicity and pyrogenicity. Indeed, a main challenge in the development of protein-based nanoparticles is finding effective procedures to remove endotoxins without affecting protein stability, since every intravenous injectable formulation that should be assessed in preclinical and clinical phase studies should display endotoxins concentration below the admitted limit of 5 EU/kg. Different strategies could be employed to achieve such a result, either by using affinity chromatography or detergents. However, these strategies are not applicable to protein nanocages as such and require implementations. Here we propose a combined protocol to remove bacterial endotoxins from nanocages of human H-ferritin, which is one of the most studied and most promising protein-based drug delivery systems. This protocol couples the affinity purification with the Endotrap HD resin to a treatment with Triton X-114. Exploiting this protocol, we were able to obtain excellent levels of purity maintaining good protein recovery rates, without affecting nanocage interactions with target cells. Indeed, binding assay and confocal microscopy experiments confirm that purified H-ferritin retains its capability to specifically recognize cancer cells. This procedure allowed to obtain injectable formulations, which is preliminary to move to a clinical trial.

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