EVM and Achievable Data Rate Analysis of Clipped OFDM Signals in Visible Light Communication

Orthogonal frequency division multiplexing (OFDM) has been considered for visible light communication (VLC) thanks to its ability to boost data rates as well as its robustness against frequency-selective fading channels. A major disadvantage of OFDM is the large dynamic range of its time-domain waveforms, making OFDM vulnerable to nonlinearity of light emitting diodes (LEDs). DC biased optical OFDM (DCO-OFDM) and asymmetrically clipped optical OFDM (ACO-OFDM) are two popular OFDM techniques developed for the VLC. In this paper, we will analyze the performance of the DCO-OFDM and ACO-OFDM signals in terms of error vector magnitude (EVM), signal-to-distortion ratio (SDR), and achievable data rates under both average optical power and dynamic optical power constraints. EVM is a commonly used metric to characterize distortions. We will describe an approach to numerically calculate the EVM for DCO-OFDM and ACO-OFDM. We will derive the optimum biasing ratio in the sense of minimizing EVM for DCO-OFDM. Additionally, we will formulate the EVM minimization problem as a convex linear optimization problem and obtain an EVM lower bound against which to compare the DCO-OFDM and ACO-OFDM techniques. We will prove that the ACO-OFDM can achieve the lower bound. Average optical power and dynamic optical power are two main constraints in VLC. We will derive the achievable data rates under these two constraints for both additive white Gaussian noise (AWGN) channel and frequency-selective channel. We will compare the performance of DCO-OFDM and ACO-OFDM under different power constraint scenarios

Surface reconstruction induced geometries of Si clusters

We discuss a generalization of the surface reconstruction arguments for the structure of intermediate size Si clusters, which leads to model geometries for the sizes 33, 39 (two isomers), 45 (two isomers), 49 (two isomers), 57 and 61 (two isomers). The common feature in all these models is a structure that closely resembles the most stable reconstruction of Si surfaces, surrounding a core of bulk-like tetrahedrally bonded atoms. We investigate the energetics and the electronic structure of these models through first-principles density functional theory calculations. These models may be useful in understanding experimental results on the reactivity of Si clusters and their shape as inferred from mobility measurements.Comment: 9 figures (available from the author upon request) Submitted to Phys. Rev.

The Structure of the Chemokine Receptor CXCR1 in Phospholipid Bilayers and Interactions with IL-8

CXCR1 is one of two high-affinity receptors for the CXC chemokine interleukin-8 (IL-8), a major mediator of immune and inflammatory responses implicated in many disorders, including tumor growth(1-3). IL-8, released in response to inflammatory stimuli, binds to the extracellular side of CXCR1. The ligand-activated intracellular signaling pathways result in neutrophil migration to the site of inflammation(2). CXCR1 is a class-A, rhodopsin-like G-protein-coupled receptor (GPCR), the largest class of integral membrane proteins responsible for cellular signal transduction and targeted as drug receptors(4-7). Despite its importance, its molecular mechanism is poorly understood due to the limited structural information available. Recently, structure determination of GPCRs has advanced by tailoring the receptors with stabilizing mutations, insertion of the protein T4 lysozyme and truncations of their amino acid sequences(8), as well as addition of stabilizing antibodies and small molecules(9) that facilitate crystallization in cubic phase monoolein mixtures(10). The intracellular loops of GPCRs are critical for G-protein interactions(11) and activation of CXCR1 involves both N-terminal residues and extracellular loops(2,12,13). Our previous NMR studies indicate that IL-8 binding to the N-terminal residues is mediated by the membrane, underscoring the importance of the phospholipid bilayer for physiological activity(14). Here we report the three-dimensional structure of human CXCR1 determined by NMR spectroscopy. The receptor is in liquid crystalline phospholipid bilayers, without modification of its amino acid sequence and under physiological conditions. Features important for intracellular G-protein activation and signal transduction are revealed