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Silicon --- Passivation. --- -Passivation. --- -Silicium --- Group 14 elements --- Passivation of integrated circuits --- Passivity (Chemistry) --- Protective coatings --- Passivation --- Electronics and optics of solids --- Integrated circuits --- Electric properties --- Electric properties. --- Nonmetals --- -Passivation of integrated circuits --- Silicium --- Silicon - Electric properties --- Integrated circuits - Passivation --- -Passivation

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Polycrystalline semiconductors. --- Integrated circuits --- Solar cells. --- Passivation.

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Silicon technology today forms the basis of a world-wide, multi-billion dollar component industry. The reason for this expansion can be found not only in the physical properties of silicon but also in the unique properties of the silicon-silicon dioxide interface. However, silicon devices are still subject to undesired electrical phenomena called ""instabilities"". These are due mostly to the imperfect nature of the insulators used, to the not-so-perfect silicon-insulator interface and to the generation of defects and ionization phenomena caused by radiation. The problem of instabilities is

Integrated circuits -- Passivation. --- Integrated circuits. --- Silicon -- Electric properties.

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Silicon --- Crystal growth --- Energy Accounting. --- Silicon Solar Cells. --- Fabrication. --- Silicon. --- Mechanical Properties. --- Impurities. --- Contractors. --- Gettering. --- Manufacturing. --- Passivation. --- Defects. --- Solar Cells. --- Microelectronics. --- Defects --- Si Solar Cell --- Crystalline Solar Cell --- Materials And Processes

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Protein adsorption to solids, nanomaterials, and biological surfaces is of central interest in many fields, including biomedicine, bioanalytical chemistry, materials engineering, bio-nanotechnology, and basic biomolecular research. Although protein adsorption may sometimes occur with little consequence on molecular structure, interactions with surfaces frequently cause changes in local or global conformations and dynamics, perturbations to secondary structures or tertiary folds, eventually resulting in dramatically altered protein function. Importantly, surfaces may trigger protein misfolding and self-aggregation, or, conversely, promote protein structure formation. The use of nanoscale surfaces to remodel the conformational landscape and the aggregation pathways of amyloidogenic peptides and proteins has been proposed as a promising strategy against several severe human diseases. The rapid growth of applications and technological innovation which is based on or concerned with protein adsorption necessitates renewed efforts to provide molecular-level insights into adsorption-induced protein structural perturbations. In this Special Issue, we gathered the recent findings of experimental and computational investigations that contributed novel insights into protein adsorption with a focus on the structural and dynamic aspects of proteins.

Research & information: general --- Biology, life sciences --- Biochemistry --- sarcoplasmic reticulum Ca2+-ATPase --- Cu+-ATPase --- phospholipid flippase --- charge displacement --- concentration jump --- solid supported membrane --- conformational transition --- electrogenicity --- ion translocation --- phospholipid flipping --- protein-nanoparticle interactions --- protein NMR --- amyloidogenic proteins --- nitroxide paramagnetic perturbation --- spin label extrinsic probes --- Tempol --- β2-microglobulin --- protein conformation --- protein-surface association --- lipid membranes --- surface-immobilized protein --- EPR spectroscopy --- alpha-synuclein --- amyloid fibrils --- conformational flexibility --- protein adsorption --- protein aggregation --- nano-bio interface --- nanocomposite --- nanoparticles --- supramolecular assembly --- NMR spectroscopy --- gold nanoparticles --- PEGylation --- adsorption --- passivation --- sarcoplasmic reticulum Ca2+-ATPase --- Cu+-ATPase --- phospholipid flippase --- charge displacement --- concentration jump --- solid supported membrane --- conformational transition --- electrogenicity --- ion translocation --- phospholipid flipping --- protein-nanoparticle interactions --- protein NMR --- amyloidogenic proteins --- nitroxide paramagnetic perturbation --- spin label extrinsic probes --- Tempol --- β2-microglobulin --- protein conformation --- protein-surface association --- lipid membranes --- surface-immobilized protein --- EPR spectroscopy --- alpha-synuclein --- amyloid fibrils --- conformational flexibility --- protein adsorption --- protein aggregation --- nano-bio interface --- nanocomposite --- nanoparticles --- supramolecular assembly --- NMR spectroscopy --- gold nanoparticles --- PEGylation --- adsorption --- passivation