1,721,223 research outputs found
Microscopic theory of vertical-transport phenomena in semiconductor heterostructures: Interplay between two- and three-dimensional hot-carrier relaxation
Full text linkA theoretical analysis of vertical-transport phenomena in semiconductor heterostructures is presented. In particular, the scattering coupling between two- and three-dimensional states in multiple quantum wells is investigated. To this purpose, a fully three-dimensional approach for the description of both localized and extended states in the heterostructure is proposed. Starting from such three-dimensional states, obtained from a self-consistent Schrödinger-Poisson calculation, a Monte Carlo solution of the corresponding Boltzmann transport equation is performed. In contrast to various phenomenological transport models, the present simulation scheme allows a kinetic description, i.e., based on microscopic scattering rates, of vertical transport across a generic heterostructure. Our results provide a rigorous description of hot-carrier relaxation between extended and localized states. This simulation scheme has been applied to finite multiple quantum wells with different geometries and doping profiles. A detailed analysis of the electron current as a function of temperature in quasiequilibrium conditions shows good agreement with experimental results. Moreover, in non-equilibrium conditions (i.e., hot-carrier regime) the scattering coupling between three- and two-dimensional states is found to play a significant role in modifying the carrier mobility as well as the fraction of conducting electrons
Quantitative optical lock-in detection for quantitative imaging of switchable and non-switchable components
No full textReversible photoswitching has been proposed as a way to identify molecules that are present in small numbers over a large, non-switching, background. This approach, called optical-lock-indetection (OLID) requires the deterministic control of the fluorescence of a photochromic emitter through optical modulation between a bright (on) and a dark state (off). OLID yields a high-contrast map where the switching molecules are pinpointed, but the fractional intensities of the emitters are not returned. The present work presents a modified OLID approach (quantitative OLID or qOLID) that yields quantitative information of the switching (f(SW)) and non-switching (f(NS)) components. After the validation of the method with a sample dataset and image sequence, we apply qOLID to measurements in cells that transiently express the photochromic protein EYQ1. We show that qOLID is efficient in separating the modulated from the non-modulated signal, the latter deriving from background/autofluorescence or fluorophores emitting in the same spectral region. Finally, we apply qOLID to Forster (Fluorescence) Resonance Energy Transfer (FRET) imaging. We here demonstrate that qOLID is able to highlight the distribution of FRET intensity in a sample by using a photochromic donor and a non-photochromic acceptor
Development and In Vivo Application of a Novel Family of Dendrimer-Based Fluorescent Biosensors
No full textManipulation of Electron Orbitals in Hard-Wall InAs/InP Nanowire Quantum Dots RID C-6303-2008
No full textWe present a novel technique for the manipulation of the energy, spectrum of hard wall InAs/InP nanowire quantum dots. By using two local gate electrodes, we induce a strong transverse electric field in the dot and demonstrate the controlled modification of its electronic orbitals. Our approach allows us to dramatically enhance the single particle energy spacing between the first two quantum levels in the dot and thus to increment the working temperature of our InAs/InP single electron transistors. Our devices display a very robust modulation of the conductance even at liquid nitrogen temperature, while allowing an ultimate control of the electron filling down to the last free carrier. Potential further applications of the technique to time-resolved spin manipulation are also discussed
Fluorescence recovery after photobleaching reveals the biochemistry of nucleocytoplasmic exchange
No full textFluorescence recovery after photobleaching (FRAP) can help unveil subtle dynamical and biochemical properties of intracellular components. A peculiar aspect of this method is that it is based on the change of optical properties only, whereas dynamics and biochemistry of the molecules of interest are not perturbed. This makes FRAP particularly suitable for the study of protein translocation, e.g., between nucleus and cytoplasm. Here we present a comprehensive theoretical treatment of FRAP applied to protein nucleocytoplasmic translocation by passive diffusion and/or energy-driven processes across the nuclear envelope. Our mathematical model is validated by experimental FRAP studies with functionalized fluorescent protein chimeras. Using this approach we demonstrate that molecular crowding at the nuclear pore does not hamper passive diffusion and calculate the dimension of the nuclear pore size (5.33 nm). Additionally, our FRAP analysis reveals the biochemical parameters (maximum translocation rate and dissociation constant of the transport complex in cytoplasm) associated with the active import of a prototypical nuclear localization sequence (NLS of SV40) and related mutants. We demonstrate that transportin binding and active import into the nucleus are independent processes that can be separately modulated. The present results are discussed in light of their potential to help in engineering sequences for intracellular targeted delivery of sensors and/or therapeutic compounds. Finally, the limits of validity of our mathematical model are addressed. RI Bizzarri, Ranieri/H-1779-201
Probing Nuclear Localization Signal-Importin alpha Binding Equilibria in Living Cells
No full textThe regulated process of protein import into the nucleus of a eukaryotic cell is mediated by specific nuclear localization signals (NLSs) that are recognized by protein-import receptors. In this study, we present fluorescence-based methods to quantitatively address the physicochemical details of NLS recognition by the receptor protein importin alpha (Imp alpha) in living cells. First, by combining fluorescence recovery after photobleaching measurements and protein-concentration calibration, we quantitatively define nuclear import saturability and afford an affinity value for NLS-Imp alpha binding. Second, by fluorescence lifetime imaging microscopy, we directly monitor the occurrence of NLS-Imp alpha interaction and measure its effective dissociation constant (K(D)) in the actual cellular environment. Our kinetic and thermodynamic analyses independently indicate that the subsaturation of Imp alpha with the expressed NLS cargo regulates nuclear import rates in living cells, in contrast to what can be predicted on the basis of available in vitro data. Finally, our experiments also provide evidence for the regulation of nuclear import mediated by the intrasteric importin beta-binding domain of Imp alpha and yield the first estimate of its autoinhibition energy in living cells
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