On-Line Monitoring of Mechanical Faults in Variable-Speed Induction Motor Drives Using the Wigner Distribution

This paper deals with the detection of mechanical load faults in induction motors during speed transients. The detection strategy is based on stator current analysis. Mechanical load faults generally lead to load torque oscillations at specific frequencies related to the mechanical rotor speed. The torque oscillations produce a characteristic sinusoidal phase modulation of the stator current. Speed transients result in time-varying supply frequencies that prevent the use of classical, Fourier transform-based spectral estimation. This paper proposes the use of a time-frequency distribution, the Wigner Distribution, for stator current analysis. Fault indicators are extracted from the distribution for on-line condition monitoring. The proposed methods are implemented on a low-cost digital signal processor. Experimental results in a steady-state and during transients with load torque oscillations and load imbalance are presented.     

3H](azidophenyl)ureido taxoid photolabels peptide amino acids 281-304 of alpha-tubulin

The taxoid binding site on porcine brain tubulin was covalently labeled, in the presence or absence of Taxotere, with the photoaffinity reagent [3H]-p-(azidophenyl)ureido taxoid derivative [3H]TaxAPU [Combeau, C., Commercon, A., Mioskowski, C., Rousseau, B., Aubert, F., & Goeldner, M. (1994) Biochemistry 33, 6676-6683]. After disulfide reduction and carboxymethylation, the alkylated tubulin samples were treated with trypsin and the mixtures of peptides were first fractionated by gel filtration over Sephadex G50. Anion exchange chromatography of the radioactive areas showed, for one area, three major radioactive signals which were further analyzed by reversed phase C18 HPLC, leading to well-resolved radioactive peaks. Microsequencing of these different peaks gave a complete sequence of a tryptic fragment on alpha-tubulin (alpha-281-304) and two partial peptide sequences of a tryptic fragment on beta-tubulin (beta-217-229) in addition to sequences of mixture of peptides. The radioactive signals were lost while concentrating the samples for microsequencing, preventing the identification of the modified amino acids. These results identify the first peptide on alpha-tubulin which binds to the taxoids and confirm the involvement of both alpha- and beta-tubulin in the taxoid binding site.