Modifying Existing 138-kV Transmission Towers to 230-kV Capacity

Wood, Basil; Moore, Travis L.

doi:10.1109/tdc.2006.1668663

Cited by 2 publications

(3 citation statements)

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“…We postulated that this mass mis-match could be caused by an amidation event, such as the switch from aspartic acid to asparagine or glutamic acid to glutamine. 45 We evaluated appropriate matches for the theoretical monoisotopic mass (based on reported Uniprot protein sequence) to the experimentally measured monoisotopic mass by mass error and quality fit of the theoretical isotopomer envelope to the experimental isotopomer envelope ( Figure S7). When we made a change of one amino acid in the theoretical sequence (D → N), we were able to match the experimentally measured mass and theoretical mass of CKM and CKS more confidently, based on the aforementioned metrics ( Figure S7).…”

Section: Ft-icr Ms Analysis Of Ssec Fractionsmentioning

confidence: 99%

“…We analyzed fraction 8 collected from sSEC fractionation of pig heart tissue extract and isolated intermediate size (32)(33)(34)(35)(36)(37)(38)(39)(40)(41)(42)(43)(44)(45)(46)(47) proteins for top-down analysis ( Figure 4A). For MDH and CKM, we selected the highest abundance ions with the highest charge (34+ and 44+, respectively), since ECD fragmentation is more efficient for higher-charged protein ions.…”

Section: Sequence Characterization Of Metabolic Enzymesmentioning

confidence: 99%

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A Top-Down Proteomics Platform Coupling Serial Size Exclusion Chromatography and Fourier Transform Ion Cyclotron Resonance Mass Spectrometry

et al. 2019

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Mass spectrometry (MS)-based top-down proteomics provides rich information about proteoforms arising from combinatorial amino acid sequence variations and post-translational modifications (PTMs). Fourier transform ion cyclotron resonance (FT-ICR) MS affords ultra-high resolving power and provides high-accuracy mass measurements, presenting a powerful tool for top-down MS characterization of proteoforms. However, detection and characterization of large proteins from complex mixtures remain challenging due to the exponential decrease in S:N with increasing molecular weight (MW) and co-eluting low-MW proteins; thus, size-based fractionation of complex protein mixtures prior to MS analysis is necessary. Here, we directly combine MScompatible serial size exclusion chromatography (sSEC) fractionation with 12 T FT-ICR MS for targeted top-down characterization of proteins from complex mixtures extracted from the human and swine heart proteome. Benefiting from the ultra-high resolving power of FT-ICR, we isotopically resolved 31 distinct proteoforms (30-50 kDa) simultaneously in a single mass spectrum within a 100 m/z window. Notably, within a 5 m/z window, we obtained baseline isotopic resolution for 6 distinct large proteoforms (30-50 kDa). The ultra-high resolving power of FT-ICR MS combined with sSEC fractionation enabled targeted top-down analysis of large proteoforms (>30 kDa) from the human heart proteome without extensive chromatographic separation or protein purification. Further separation of proteoforms inside of the mass spectrometer (in-MS) allowed for isolation of individual proteoforms for targeted electron capture dissociation (ECD) for high sequence coverage. sSEC/FT-ICR ECD facilitated identification and sequence characterization of important metabolic enzymes. This platform, which facilitates deep *

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Section: Ft-icr Ms Analysis Of Ssec Fractionsmentioning

confidence: 99%

Section: Sequence Characterization Of Metabolic Enzymesmentioning

confidence: 99%

A Top-Down Proteomics Platform Coupling Serial Size Exclusion Chromatography and Fourier Transform Ion Cyclotron Resonance Mass Spectrometry

et al. 2019

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“…Figure 10 shows the minimum clearance at 0 In 2012, Selvaraj et al published work on FRP pultruded profiles made of composite cross-arms [34,54]. In this case, FRP pultruded profiles are used [55]. The mechanical performance of the composite cross-arm was evaluated using experimental testing, an analytical solution, and a finite element simulation.…”

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confidence: 99%

Historical Review of Advancements in Insulated Cross-Arm Technology

et al. 2022

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High-voltage transmission technology has advanced quickly with the overall development and increased use of renewable energy. More demands on the insulating system are made when high-voltage power systems evolve. One of the significant factors is the sharp rise in population density, which led to the high demand for electricity. Right-of-way infringement is a problem that frequently occurs these days. Transmission is done over a rated capacity; as a result, the transmission line heats up, the insulation ages, and the electric field becomes distorted. The insulating system is prone to fail too soon when the operating voltage inverses or when there is a significant temperature differential. Environmentally friendly insulating materials have received much attention recently. A synergistic optimisation of heat resistance properties, mechanical properties, and dielectric properties must be accomplished before these materials can be used in high-voltage transmission systems. They must also withstand harsh electrical and thermal shocks such as overvoltage and short-circuit faults. One of the developments that has become a popular research topic is the constantly evolving tower design. This review article presents advancements in cross-arm technology in high-voltage transmission systems to elaborate on the limitations and contributions of different research work.

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Modifying Existing 138-kV Transmission Towers to 230-kV Capacity

Cited by 2 publications

References 1 publication

A Top-Down Proteomics Platform Coupling Serial Size Exclusion Chromatography and Fourier Transform Ion Cyclotron Resonance Mass Spectrometry

A Top-Down Proteomics Platform Coupling Serial Size Exclusion Chromatography and Fourier Transform Ion Cyclotron Resonance Mass Spectrometry

Historical Review of Advancements in Insulated Cross-Arm Technology

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