Application of calorimetric method for loss measurement of a SynRM drive system

Synchronous reluctance motors (SynRMs) are gaining in popularity in industrial drives due to their permanent magnet-free, competitive performance, and robust features. This paper studies the power losses in a 90-kW converter-fed SynRM drive by a calorimetric method in comparison of the traditional input-output method. After the converter and the motor were measured simultaneously in separate chambers, the converter was installed inside the large-size chamber next to the motor and the total drive system losses were obtained using one chamber. The uncertainty of both measurement methods is analyzed and discussed.

RT-PCR for the pseudogene-free amplification of the glyceraldehyde-3-phosphate dehydrogenase gene (gapd)

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is an enzyme which catalyses the conversion of glyceraldehyde-3-phosphate to 1,3 diphosphoglycerate. It is considered to be constitutively expressed in all cells, and as such the gene for GAPDH (gapd) is commonly used as a benchmark reference in expression studies. However, previous investigations have demonstrated that gapd may show altered gene expression in a number of disease states and under certain experimental conditions, suggesting that results of experiments using gapd as a control should be interpreted with caution. Furthermore, consideration must be given to the potential co-amplification of pseudogenes of gapd during RT-PCR. Here, we describe a method to avoid the amplification of contaminating pseudogenes through the design of primers that bind only to genuine gapd mRNA transcript. © 2003 Elsevier Ltd. All rights reserved.

Decision-directed-free blind phase noise estimation for COOFDM

We demonstrate an effective decision-directed-free blind phase noise compensation method for CO-OFDM transmission. By applying this technique, the common phase error can be accurately estimated using as few as three test phases.

Detergent-free membrane protein purification

Membrane proteins are localised within a lipid bilayer; in order to purify them for functional and structural studies the first step must involve solubilising or extracting the protein from these lipids. To date this has been achieved using detergents which disrupt the bilayer and bind to the protein in the transmembrane region. However finding conditions for optimal extraction, without destabilising protein structure is time consuming and expensive. Here we present a recently-developed method using a styrene maleic acid (SMA) co-polymer instead of detergents. The SMA co-polymer extracts membrane proteins in a small disc of lipid bilayer which can be used for affinity chromatography purification, thus enabling the purification of membrane proteins while maintaining their native lipid bilayer environment.