Helicobacter pylori, strain 26695, has a circular genome of 1,667,867 base pairs and 1,590 predicted coding sequences. Sequence analysis indicates that H. pylori has well-developed systems for motility, for scavenging iron, and for DNA restriction and modification. Many putative adhesins, lipoproteins and other outer membrane proteins were identified, underscoring the potential complexity of host-pathogen interaction. Based on the large number of sequence-related genes encoding outer membrane proteins and the presence of homopolymeric tracts and dinucleotide repeats in coding sequences, H. pylori, like several other mucosal pathogens, probably uses recombination and slipped-strand mispairing within repeats as mechanisms for antigenic variation and adaptive evolution. Consistent with its restricted niche, H. pylori has a few regulatory networks, and a limited metabolic repertoire and biosynthetic capacity. Its survival in acid conditions depends, in part, on its ability to establish a positive inside-membrane potential in low pH.

We have carried out detailed statistical analyses of integral membrane proteins of the helix-bundle class from eubacterial, archaean, and eukaryotic organisms for which genome-wide sequence data are available. Twenty to 30% of all ORFs are predicted to encode membrane proteins, with the larger genomes containing a higher fraction than the smaller ones. Although there is a general tendency that proteins with a smaller number of transmembrane segments are more prevalent than those with many, uni-cellular organisms appear to prefer proteins with 6 and 12 transmembrane segments, whereas Caenorhabditis elegans and Homo sapiens have a slight preference for proteins with seven transmembrane segments. In all organisms, there is a tendency that membrane proteins either have many transmembrane segments with short connecting loops or few transmembrane segments with large extra-membraneous domains. Membrane proteins from all organisms studied, except possibly the archaeon Methanococcus jannaschii, follow the so-called "positiveinside" rule; Le., they tend to have a higher frequency of positively charged residues in cytoplasmic than in extracytoplasmic segments.

A new, simple method for predicting transmembrane segments in integral membrane proteins has been developed. It is based on low-stringency dot-plots of the query sequence against a collection of non-homologous membrane proteins using a previously derived scoring matrix [Cserzö et al., 1994, J. Mol. Biol., 243, 388-396]. This so-called dense alignment surface (DAS) method is shown to perform on par with earlier methods that require extra information in the form of multiple sequence alignments or the distribution of positively charged residues outside the transmembrane segments, and thus improves prediction abilities when only single-sequence information is available or for classes of membrane proteins that do not follow the 'positive inside' rule.

Azotobacter vinelandii is a soil bacterium related to the Pseudomonas genus that fixes nitrogen under aerobic conditions while simultaneously protecting nitrogenase from oxygen damage. In response to carbon availability, this organism undergoes a simple differentiation process to form cysts that are resistant to drought and other physical and chemical agents. Here we report the complete genome sequence of A. vinelandii DJ, which has a single circular genome of 5,365,318 bp. In order to reconcile an obligate aerobic lifestyle with exquisitely oxygen-sensitive processes, A. vinelandii is specialized in terms of its complement of respiratory proteins. It is able to produce alginate, a polymer that further protects the organism from excess exogenous oxygen, and it has multiple duplications of alginate modification genes, which may alter alginate composition in response to oxygen availability. The genome analysis identified the chromosomal locations of the genes coding for the three known oxygen-sensitive nitrogenases, as well as genes coding for other oxygen-sensitive enzymes, such as carbon monoxide dehydrogenase and formate dehydrogenase. These findings offer new prospects for the wider application of A. vinelandii as a host for the production and characterization of oxygen-sensitive proteins.

We review common extensions of particle-in-cell (PIC) schemes which account for strong field phenomena in laser-plasma interactions. After describing the physical processes of interest and their numerical implementation, we provide solutions for several associated methodological and algorithmic problems. We propose a modified event generator that precisely models the entire spectrum of incoherent particle emission without any low-energy cutoff, and which imposes close to the weakest possible demands on the numerical time step. Based on this, we also develop an adaptive event generator that subdivides the time step for locally resolving QED events, allowing for efficient simulation of cascades. Further, we present a new and unified technical interface for including the processes of interest in different PIC implementations. Two PIC codes which support this interface, PICADOR and ELMIS, are also briefly reviewed. CONTENTS

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In this study, the effect on thin film growth due to an anomalous electron transport, found in high power impulse magnetron sputtering (HiPIMS) has been investigated for the case of a planar circular magnetron. An important consequence of this type of transport is that it affects the way ions are being transported in the plasma. It was found that a significant fraction of ions are transported radially outwards in the vicinity of the cathode, across the magnetic field lines, leading to increased deposition rates directly at the side of the cathode (perpendicular to the target surface). Furthermore, this mass transport parallel to the target surface leads to that the fraction of sputtered material reaching a substrate placed directly in front of the target is substantially lower in HiPIMS compared to conventional direct current magnetron sputtering (dcMS). This would help to explain the lower deposition rates generally observed for HiPIMS compared to dcMS. Moreover, time-averaged mass spectrometry measurements of the energy distribution of the cross-field transported ions were carried out. The measured distributions show a direction-dependent high-energy tail, in agreement with predictions of the anomalous transport mechanism.

We have analyzed the structure of mitochondrial cytochrome c oxidase in terms of general characteristics thought to be important for describing the architecture of helix bundle membrane proteins. Many aspects of the structure are similar to what has previously been found for the photosynthetic reaction center and bacteriorhodopsin. Our results lead to a considerably more precise general picture of membrane protein architecture than has hitherto been possible to obtain.