Metrological Characterization of a High-Temperature Hybrid Sensor Using Thermal Radiation and Calibrated Sapphire Fiber Bragg Grating for Process Monitoring in Harsh Environments.

Fiber Bragg gratings inscribed in single crystalline multimode sapphire fibers (S-FBG) are suitable for monitoring applications in harsh environments up to 1900 °C. Despite many approaches to optimize the S-FBG sensor, a metrological investigation of the achievable temperature uncertainties is still missing. In this paper, we developed a hybrid optical temperature sensor using S-FBG and thermal radiation signals.

Enhanced Distributed Fiber Optic Vibration Sensing and Simultaneous Temperature Gradient Sensing Using Traditional C-OTDR and Structured Fiber with Scattering Dots.

We present results demonstrating several beneficial effects on distributed fiber optic vibration sensing (DVS) functionality and performance resulting from utilizing standard single mode optical fiber (SMF) with femtosecond laser-inscribed equally-spaced simple scattering dots. This modification is particularly useful when using traditional single-wavelength amplitude-based coherent optical time domain reflectometry (C-OTDR) as sensing method. Local sensitivity is increased in quasi-distributed interferometric sensing zones which are formed by the fiber segments between subsequent pairs of the scattering dots.

Staphylococcal phosphoenolpyruvate-dependent phosphotransferase system: molecular cloning and nucleotide sequence of the Staphylococcus carnosus ptsI gene and expression and complementation studies of the gene product.

A digoxigenin-labeled DNA probe that was complementary to the gene ptsH and the beginning of the gene ptsI was used to clone a 3.2-kb HincII-BamHI restriction fragment containing the complete ptsI gene of Staphylococcus carnosus. The restriction fragment was cloned in the antisense orientation to the lac promoter in the low-copy-number vector pSU18.

Staphylococcal phosphoenolpyruvate-dependent phosphotransferase system. Purification and protein sequencing of the Staphylococcus carnosus histidine-containing protein, and cloning and DNA sequencing of the ptsH gene.

The histidine-containing protein (HPr) of the bacterial phosphoenolpyruvate-dependent phosphotransferase system (PTS) was isolated from Staphylococcus carnosus and purified to homogeneity. The protein sequence was determined by Edman degradation of peptides obtained by proteolytic digestion with proteases V8, trypsin and chemical cleavage with BrCN. Furthermore, immunological screening of a chromosomal S.

Enzyme IIIlac of the staphylococcal phosphoenolpyruvate-dependent phosphotransferase system: site-specific mutagenesis of histidine residues, biochemical characterization and 1H-NMR studies.

The lactose-specific phosphocarrier protein enzyme III of the bacterial phosphoenol-pyruvate-dependent phosphotransferase system of Staphylococcus aureus was modified by site-specific mutagenesis on the corresponding lacF gene in order to replace the histidine residues 78 and 82 of the amino acid sequence with a serine residue. Wild-type and both mutant genes were overexpressed in Escherichia coli and the gene products were purified to homogeneity. The conformation of wild-type and mutant proteins were monitored by 1H-NMR spectroscopy.