MONITORING OF CORROSION UNDER CATHODIC PROTECTION CONDITIONS UTILIZING COUPLED MULTIELECTRODE SENSORS
Real-time corrosion monitoring for carbon steel materials in simulated seawater under cathodic protection conditions was conducted, utilizing coupled multielectrode sensors. It was demonstrated that the coupled multielectrode sensor is an effective real-time tool for monitoring the effectiveness of cathodic protection and for measurement of the threshold value of the protection potential for specific equipment.
ONLINE MONITORING OF UNDERCOATING CORROSIONS UTILIZING COUPLED MULTIELECTRODE SENSORS
Online monitoring of carbon steel corrosion under different commercial coatings was conducted, utilizing coupled multielectrode sensors. The experimental results showed that the coupled multielectrode corrosion sensor is an effective tool for detecting initial defects and real-time degradation of the coatings. Because of their high sensitivity, the coupled multielectrode sensors may also be used as a quick and convenient tool for optimizing the selection of proper coatings for different applications.
A single amino acid substitution in elongation factor Tu disrupts interaction between the ternary complex and the ribosome
Elongation factor Tu (EF-Tu).GTP has the primary function of promoting the efficient and correct interaction of aminoacyl-tRNA with the ribosome. Very little is known about the elements in EF-Tu involved in this interaction. We describe a mutant form of EF-Tu, isolated in Salmonella typhimurium, that causes a severe defect in the interaction of the ternary complex with the ribosome. The mutation causes the substitution of Val for Gly-280 in domain II of EF-Tu. The in vivo growth and translation phenotypes of strains harboring this mutation are indistinguishable from those of strains in which the same tuf gene is insertionally inactivated. Viable cells are not obtained when the other tuf gene is inactivated, showing that the mutant EF-Tu alone cannot support cell growth. We have confirmed, by partial protein sequencing, that the mutant EF-Tu is present in the cells. In vitro analysis of the natural mixture of wild-type and mutant EF-Tu allows us to identify the major defect of this mutant. Our data shows that the EF-Tu is homogeneous and competent with respect to guanine nucleotide binding and exchange, stimulation of nucleotide exchange by EF-Ts, and ternary complex formation with aminoacyl-tRNA. However various measures of translational efficiency show a significant reduction, which is associated with a defective interaction between the ribosome and the mutant EF-Tu.GTP.aminoacyl-tRNA complex. In addition, the antibiotic kirromycin, which blocks translation by binding EF-Tu on the ribosome, fails to do so with this mutant EF-Tu, although it does form a complex with EF-Tu. Our results suggest that this region of domain II in EF-Tu has an important function and influences the binding of the ternary complex to the codon-programmed ribosome during protein synthesis. Models involving either a direct or an indirect effect of the mutation are discussed.