On the stator slot geometry of a cable wound generator for hydrokinetic energy conversion.

The stator slot geometry of a cable wound permanent magnet synchronous generator for hydrokinetic energy conversion is evaluated. Practical experience from winding two cable wound generators is used to propose optimized dimensions of different parts in the stator slot geometry. A thorough investigation is performed through simulations of how small geometrical changes alter the generator performance. The finite element method (FEM) is used to model the generator and the simulations show that small changes in the geometry can have large effect on the performance of the generator. Furthermore, it is concluded that the load angle is especially sensitive to small geometrical changes. A new generator design is proposed which shows improved efficiency, reduced weight, and a possibility to decrease the expensive permanent magnet material by almost one-fifth.

System efficiency of a tap transformer based grid connection topology applied on a direct driven generator for wind power.

Results from experiments on a tap transformer based grid connection system for a variable speed vertical axis wind turbine are presented. The tap transformer based system topology consists of a passive diode rectifier, DC-link, IGBT inverter, LCL-filter, and tap transformer. Full range variable speed operation is enabled by using the different step-up ratios of a tap transformer. Simulations using MATLAB/Simulink have been performed in order to study the behavior of the system. A full experimental set up of the system has been used in the laboratory study, where a clone of the on-site generator was driven by an induction motor and the system was connected to a resistive load to better evaluate the performance. Furthermore, the system is run and evaluated for realistic wind speeds and variable speed operation. For a more complete picture of the system performance, a case study using real site Weibull parameters is done, comparing different tap selection options. The results show high system efficiency at nominal power and an increase in overall power output for full tap operation in comparison with the base case, a standard transformer. In addition, the loss distribution at different wind speeds is shown, which highlights the dominant losses at low and high wind speeds. Finally, means for further increasing the overall system efficiency are proposed.

Development, evaluation and application of tripeptidyl-peptidase II sequence signatures.

Tripeptidyl-peptidase II (TPP II) is a cytosolic peptidase that has been implicated in fat formation and cancer, apparently independent of the enzymatic activity. In search for alternative functional regions, conserved motifs were identified and eleven signatures were constructed. Seven of the signatures covered previously investigated residues, whereas the functional importance of the other motifs is unknown. This provides directions for future investigations of alternative activities of TPP II. The obtained signatures provide an efficient bioinformatic tool for the identification of TPP II homologues. Hence, a TPP II sequence homologue from fission yeast, Schizosaccharomyces pombe, was identified and demonstrated to encode the TPP II-like protein previously reported as multicorn. Furthermore, an homologous protein was found in the prokaryote Blastopirellula marina, albeit the TPP II function was apparently not conserved. This gene is probably the result of a rare gene transfer from eukaryote to prokaryote.

Investigation of a role for Glu-331 and Glu-305 in substrate binding of tripeptidyl-peptidase II.

The aim of this study was to investigate the mechanism by which tripeptidyl-peptidase II (TPP II) can specifically release tripeptides from the free N-terminus of an oligopeptide. The subtilisin-like N-terminal part of TPP II was modelled using subtilisin as template. Two glutamate residues (Glu-305 and Glu-331) appeared to be positioned so as to interact with the positively charged N-terminus of the substrate. In order to test this potential interaction, both residues were replaced by glutamine and lysine. The catalytic efficiency was reduced 400-fold for the E331Q variant and 20000-fold for the E331K variant, compared with the wild-type (wt). A substantial part of this reduction was due to decreased substrate affinity, since the K(M) for both mutants was at least two orders of magnitude greater than for the wt. This decrease was linked specifically to interaction with the free N-terminal amino group, based on inhibition studies. Glu-305 appears to be essential for enzymatic activity, but the extremely low activity of the E305Q variant prevented an investigation of the involvement of Glu-305 in substrate binding. The present work is, to our knowledge, the first report to investigate a mechanism for a tripeptidyl-peptidase activity through site-directed mutagenesis.