Metalorganic Chemical Vapor Deposition Growth of High-Quality InAs/GaSb Type II Superlattices for Mid-IR Photodetector Applications
X. B. Zhang , A. Petschke, S. Mou , C. Xu , J. H. Ryou , S. L. Chuang , K. C. Hsieh, and R. D. Dupuis 1) Center for Compound Semiconductors and School of Electrical and Computer Engineering, Georgia Institute of Technology, 777 Atlantic Drive NW, Atlanta, GA, 30332-0250, USA 2) Micro and Nanotechnology Laboratory, University of Illinois at Urbana-Champaign, 208 North Wright Street, Urbana, IL 61801, USA
Uncooled InAs-GaSb type-II infrared detectors grown on GaAs substrates for the 8-12-/spl mu/m atmospheric window
We report on the growth and characterization of type-II infrared detectors with an InAs-GaSb superlattice active layer for the 8-12-/spl mu/m atmospheric window at 300 K. The material was grown by molecular beam epitaxy on semi-insulating GaAs substrates. Photoconductive detectors fabricated from the superlattices showed 80% cutoff at about 12 /spl mu/m at room temperature. The responsivity of the device is about 2 mA/W with a 1-V bias (E=5 V/cm) and the maximum measured detectivity of the device is 1.3/spl times/10/sup 8/ cm.Hz/sup 1/2//W at 11 /spl mu/m at room temperature. The detector shows very weak temperature sensitivity. Also, the extracted effective carrier lifetime, /spl tau/=26 ns, is an order of magnitude longer than the carrier lifetime in HgCdTe with similar bandgap and carrier concentration.
Negatively charged phospholipids trigger the interaction of a bacterial Tat substrate precursor protein with lipid monolayers.
Folded proteins can be translocated across biological membranes via the Tat machinery. It has been shown in vitro that these Tat substrates can interact with membranes prior to translocation. Here we report a monolayer and infrared reflection-absorption spectroscopic (IRRAS) study of the initial states of this membrane interaction, the binding to a lipid monolayer at the air/water interface serving as a model for half of a biological membrane. Using the model Tat substrate HiPIP (high potential iron-sulfur protein) from Allochromatium vinosum, we found that the precursor preferentially interacts with monolayers of negatively charged phospholipids. The signal peptide is essential for the interaction of the precursor protein with the monolayer because the mature HiPIP protein showed no interaction with the lipid monolayer. However, the individual signal peptide interacted differently with the monolayer compared to the complete precursor protein. IRRA spectroscopy indicated that the individual signal peptide forms mainly aggregated β-sheet structures. This β-sheet formation did not occur for the signal peptide when being part of the full length precursor. In this case it adopted an α-helical structure upon membrane insertion. The importance of the signal peptide and the mature domain for the membrane interaction is discussed in terms of current ideas of Tat substrate-membrane interactions.