Characterization of gasoline/ethanol blends by infrared and excess infrared spectroscopy

This work was supported by the Northern Research Partnership (NRP) in Scotland and the Scottish Sensor Systems Centre (SSSC) funded by the Scottish Funding Council (SFC).Peer reviewedPostprin

Artificial Intelligence in Supply Chain Management: Investigation of Transfer Learning to Improve Demand Forecasting of Intermittent Time Series with Deep Learning

Demand forecasting intermittent time series is a challenging business problem. Companies have difficulties in forecasting this particular form of demand pattern. On the one hand, it is characterized by many non-demand periods and therefore classical statistical forecasting algorithms, such as ARIMA, only work to a limited extent. On the other hand, companies often cannot meet the requirements for good forecasting models, such as providing sufficient training data. The recent major advances of artificial intelligence in applications are largely based on transfer learning. In this paper, we investigate whether this method, originating from computer vision, can improve the forecasting quality of intermittent demand time series using deep learning models. Our empirical results show that, in total, transfer learning can reduce the mean square error by 65 percent. We also show that especially short (65 percent reduction) and medium long (91 percent reduction) time series benefit from this approach

The SWISS-MODEL Repository and associated resources

SWISS-MODEL Repository (http://swissmodel.expasy.org/repository/) is a database of 3D protein structure models generated by the SWISS-MODEL homology-modelling pipeline. The aim of the SWISS-MODEL Repository is to provide access to an up-to-date collection of annotated 3D protein models generated by automated homology modelling for all sequences in Swiss-Prot and for relevant models organisms. Regular updates ensure that target coverage is complete, that models are built using the most recent sequence and template structure databases, and that improvements in the underlying modelling pipeline are fully utilised. As of September 2008, the database contains 3.4 million entries for 2.7 million different protein sequences from the UniProt database. SWISS-MODEL Repository allows the users to assess the quality of the models in the database, search for alternative template structures, and to build models interactively via SWISS-MODEL Workspace (http://swissmodel.expasy.org/workspace/). Annotation of models with functional information and cross-linking with other databases such as the Protein Model Portal (http://www.proteinmodelportal.org) of the PSI Structural Genomics Knowledge Base facilitates the navigation between protein sequence and structure resource

The SWISS-MODEL Repository and associated resources

SWISS-MODEL Repository (http://swissmodel.expasy.org/repository/) is a database of 3D protein structure models generated by the SWISS-MODEL homology-modelling pipeline. The aim of the SWISS-MODEL Repository is to provide access to an up-to-date collection of annotated 3D protein models generated by automated homology modelling for all sequences in Swiss-Prot and for relevant models organisms. Regular updates ensure that target coverage is complete, that models are built using the most recent sequence and template structure databases, and that improvements in the underlying modelling pipeline are fully utilised. As of September 2008, the database contains 3.4 million entries for 2.7 million different protein sequences from the UniProt database. SWISS-MODEL Repository allows the users to assess the quality of the models in the database, search for alternative template structures, and to build models interactively via SWISS-MODEL Workspace (http://swissmodel.expasy.org/workspace/). Annotation of models with functional information and cross-linking with other databases such as the Protein Model Portal (http://www.proteinmodelportal.org) of the PSI Structural Genomics Knowledge Base facilitates the navigation between protein sequence and structure resources

Infrared spectroscopy of bilberry extract water-in-oil emulsions: Sensing the Water-Oil Interface

Water-in-oil (w/o) emulsions are of great interest in many areas of the life sciences, including food technology, bioprocess engineering, and pharmaceuticals. Such emulsions are complex multi-component systems and the molecular mechanisms which lead to a stable emulsion are yet to be fully understood. In this work, attenuated total reflection (ATR) infrared (IR) spectroscopy is applied to a series of w/o emulsions of an aqueous anthocyanin-rich bilberry extract dispersed in a medium chain triglyceride (MCT) oil phase. The content of the emulsifier polyglycerin-polyricinoleat (PGPR) has been varied systematically in order to investigate whether or not its concentration has an impact on the molecular stabilization mechanisms. The molecular stabilization is accessed by a careful analysis of the IR spectrum, where changes in the vibrational frequencies and signal strengths indicate alterations of the molecular environment at the water/oil interface. The results suggest that adding emulsifier in excess of 1% by weight does not lead to an enhanced stabilization of the emulsion

Responsibility and verification: Importance value in temporal logics

We aim at measuring the influence of the nondeterministic choices of a part of a system on its ability to satisfy a specification. For this purpose, we apply the concept of Shapley values to verification as a means to evaluate how important a part of a system is. The importance of a component is measured by giving its control to an adversary, alone or along with other components, and testing whether the system can still fulfill the specification. We study this idea in the framework of model-checking with various classical types of linear-time specification, and propose several ways to transpose it to branching ones. We also provide tight complexity bounds in almost every case.Comment: 22 pages, 12 figure

50 Hz X‐Ray Diffraction Stress Analysis and Numerical Process Simulation at Laser Surface Line Hardening of Web Structures

In situ synchrotron X-ray diffraction experiments were carried out during laser surface line hardening of the common tempering steel AISI 4140 at beamline P05@PETRA III operated by Helmholtz-Zentrum Geesthacht at the Deutsches Elektronen Synchrotron, Hamburg, Germany. A unique process chamber was used to investigate the phase and transverse surface stress evolution during a laser line hardening processes. Synchrotron radiation, in combination with microstrip line detectors, allows for a time resolution of 50 Hz. Specimen geometries were hardened using a high-power diode laser under control of the surface temperature and constant laser beam feed. Herein, it is focused on web-structured specimens in contrast to a flat geometry. The experimental results are discussed with regard to the workpiece geometry effect of the web structure dimensions on the temporal and spatial stress evolution. In addition, numerical process simulations based on the finite element method were carried out to support the drawn conclusions. The presented model is able to predict the surface transverse stresses inside the process zone center, while providing further 3D information. A heat build-up in the web leads to a wider and deeper process zone, however, the absolute hardness increase and the transverse residual stresses at the surface center are not affected

No Differences in Renal Function between Balanced 6% Hydroxyethyl Starch (130/0.4) and 5% Albumin for Volume Replacement Therapy in Patients Undergoing Cystectomy: a Randomized Controlled Trial

BACKGROUND The use of artificial colloids has declined in critical care, whereas they are still used in perioperative medicine. Little is known about the nephrotoxic potential in noncritically ill patients during routine surgery. The objective of this trial was to evaluate the influences of albumin 5% and balanced hydroxyethyl starch 6% (130/0.4) on renal function and kidney injury. METHODS One hundred urologic patients undergoing elective cystectomy were randomly assigned for this prospective, single-blinded, controlled study with two parallel groups to receive either albumin 5% or balanced hydroxyethyl starch 6% (130/0.4) as the only perioperative colloid. The primary endpoint was the ratio of serum cystatin C between the last visit at day 90 and the first preoperative visit. Secondary endpoints were estimated glomerular filtration rate and serum neutrophil gelatinase-associated lipocalin until the third postoperative day and risk, injury, failure, loss, and end-stage renal disease criteria at postoperative days 3 and 90. RESULTS The median cystatin C ratio was 1.11 (interquartile range, 1.01 to 1.23) in the albumin and 1.08 (interquartile range, 1.00 to 1.20) in the hydroxyethyl starch group (median difference = 0.03; 95% CI, -0.09 to 0.08; P = 0.165). Also, there were no significant differences concerning serum cystatin C concentrations; estimated glomerular filtration rate; risk, injury, failure, loss, and end-stage renal disease criteria; and neutrophil gelatinase-associated lipocalin. Infusion requirements, transfusion rates, and perioperative hemodynamics were similar in both groups. CONCLUSIONS With respect to renal function and kidney injury, this study indicates that albumin 5% and balanced hydroxyethyl starch 6% have comparable safety profiles in noncritically ill patients undergoing major surgery

The Protein Model Portal

Structural Genomics has been successful in determining the structures of many unique proteins in a high throughput manner. Still, the number of known protein sequences is much larger than the number of experimentally solved protein structures. Homology (or comparative) modeling methods make use of experimental protein structures to build models for evolutionary related proteins. Thereby, experimental structure determination efforts and homology modeling complement each other in the exploration of the protein structure space. One of the challenges in using model information effectively has been to access all models available for a specific protein in heterogeneous formats at different sites using various incompatible accession code systems. Often, structure models for hundreds of proteins can be derived from a given experimentally determined structure, using a variety of established methods. This has been done by all of the PSI centers, and by various independent modeling groups. The goal of the Protein Model Portal (PMP) is to provide a single portal which gives access to the various models that can be leveraged from PSI targets and other experimental protein structures. A single interface allows all existing pre-computed models across these various sites to be queried simultaneously, and provides links to interactive services for template selection, target-template alignment, model building, and quality assessment. The current release of the portal consists of 7.6million model structures provided by different partner resources (CSMP, JCSG, MCSG, NESG, NYSGXRC, JCMM, ModBase, SWISS-MODEL Repository). The PMP is available at http://www.proteinmodelportal.org and from the PSI Structural Genomics Knowledgebas

SWISS-MODEL: modelling protein tertiary and quaternary structure using evolutionary information

Protein structure homology modelling has become a routine technique to generate 3D models for proteins when experimental structures are not available. Fully automated servers such as SWISS-MODEL with user-friendly web interfaces generate reliable models without the need for complex software packages or downloading large databases. Here, we describe the latest version of the SWISS-MODEL expert system for protein structure modelling. The SWISS-MODEL template library provides annotation of quaternary structure and essential ligands and co-factors to allow for building of complete structural models, including their oligomeric structure. The improved SWISS-MODEL pipeline makes extensive use of model quality estimation for selection of the most suitable templates and provides estimates of the expected accuracy of the resulting models. The accuracy of the models generated by SWISS-MODEL is continuously evaluated by the CAMEO system. The new web site allows users to interactively search for templates, cluster them by sequence similarity, structurally compare alternative templates and select the ones to be used for model building. In cases where multiple alternative template structures are available for a protein of interest, a user-guided template selection step allows building models in different functional states. SWISS-MODEL is available at http://swissmodel.expasy.or