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The utilities frequently use non-ceramic insulators for live line maintenance. These insulators are not always tested electrically during manufacture. Undetected internal failures in an insulator may endanger workers performing live line maintenance on the insulators. The live line maintenance requires careful testing of each insulator before use. For the selection of the most effective test method, insulators were purposely made with internal flaws and then subjected to megger, hot stick, partial discharge and RIV tests as well as measurement of the total and surface component of leakage current, together with surface heating measurement. The most sensitive method is the RIV test, which identified 6 insulators with flaws. The partial discharge and hot stick tests found 4 insulators with embedded wire. From a practical point of view, the modified hot stick test seems to be suitable for field test of the insulators. Key words: hot line tools, nonceramic insulators, testing

This paper presents a technique for laboratory characterization of instrument transformers designed for transmission level voltage and current measurements. The technique is also extended to Transient Event Recorders (TERs). The objective of the method is to determine the suitability of existing substation instrument transformers for harmonic measurements, particularly in the frequency range of 60 to 1500 Hz covering the first 25 harmonics. Specifically, the following characteristics are of interest in the frequency range of 60 to 1500 Hz: transfer function magnitude and phase, linearity, and sensitivity of the frequency response to burdens. The measurement technique is based on exciting the instrument transformer primary with an impulsive waveform. Both input and output waveforms are recorded using laboratory grade probes and digitizers. Subsequently, digital signal processing techniques are used to compute the instrument transformer frequency response. Several voltage transformers (both PTs and CCVTs) and current transformers in the 230kV-765kV voltage range were tested. The results of these tests are described in the paper. Conclusions are presented regarding the suitability of the instrument transformers and transient event recorders for harmonic measurement and the requirements for such a system. A quantitative analysis of the measurement accuracy and software based methods to enhance the measurement accuracy is also presented.

We have used circular dichroism and frequency-domain fluorescence spectroscopy to determine how the site-specific substitution of Tyr138 with either Phe138 or Gln138 affects the structural coupling between the opposing domains of calmodulin (CaM). A double mutant was constructed involving conservative substitution of Tyr99 --> Trp99 and Leu69 --> Cys69 to assess the structural coupling between the opposing domains, as previously described [Sun, H., Yin, D., and Squier, T. C. (1999) Biochemistry 38, 12266-12279]. Trp99 acts as a fluorescence resonance energy transfer (FRET) donor in distance measurements to probe the conformation of the central helix. Cys69 provides a reactive group for the covalent attachment of 5-((((2-iodoacetyl)amino)ethyl)amino)naphthalene-1-sulfonic acid (IAEDANS), which functions as a FRET acceptor and permits the measurement of the rotational dynamics of the amino-terminal domain. These CaM mutants demonstrate normal calcium-dependent gel-mobility shifts and changes in their near-UV CD spectra, have similar secondary structures to wild-type CaM following calcium activation, and retain the ability to fully activate the plasma membrane Ca-ATPase. The global folds, therefore, of both the carboxyl- and amino-terminal domains in these CaM mutants are similar to that of wild-type CaM. However, in comparison to wild-type CaM, the substitution of Tyr138 with either Phe138 or Gln138 results in (i) alterations in the average spatial separation and increases in the conformational heterogeneity between the opposing globular domains and (ii) the independent rotational dynamics of the amino-terminal domain. These results indicate that alterations in either the hydrogen bond between Tyr138 and Glu82 or contact interactions between aromatic amino acid side chains have the potential to initiate the structural collapse of CaM normally associated with target protein binding and activation.