Thermal Imaging and Dimensionality Reduction Techniques for Subclinical Mastitis Detection in Dairy Sheep.

Subclinical mastitis is a common and economically significant disease that affects dairy sheep production. Thermal imaging presents a promising avenue for non-invasive detection, but existing methodologies often rely on simplistic temperature differentials, potentially leading to inaccurate assessments. This study proposes an advanced algorithmic approach integrating thermal imaging processing with statistical texture analysis and t-distributed stochastic neighbor embedding (t-SNE).

Physical unclonable functions on carbon fiber reinforced polymers using laser techniques.

We have successfully fabricated physical unclonable functions (PUF)s on carbon fiber reinforced polymers (CFRP) in the form of computer-generated holograms (CGH)s using an industrial friendly UV ns laser system. The topological randomness of the fiber network and laser absorption yield laser engraved CGH that are unique. The engraved CGH serve as PUFs and this is confirmed by the exceptionally low values of probability of cloning (POC), lower than 10, well below the commonly accepted threshold value of 10 in the literature.

Probing the Fucoxanthin-Chlorophyll /-Binding Proteins (FCPs) of the Marine Diatom sp. by Resonance Raman Spectroscopy.

We report resonance Raman spectra of the light-harvesting fucoxanthin-chlorophyll /-binding proteins (FCPs) of marine diatom sp. The Raman shifts in the N-isotope-enriched diatom provide the first spectroscopic evidence for the characterization of the C-N marker bands and, thus, of the penta- and hexacoordinated states of chlorophylls / in the FCPs. Under 405 and 442 nm Raman excitations, all of the marker bands of Chl / are observed and the isotope-based assignments provide new information concerning the structure of Chls / in the FCPs and their interactions with the protein environment.

Reversible thermally induced spin crossover in the myoglobin-nitrito adduct directly monitored by resonance Raman spectroscopy.

Myoglobin has been demonstrated to function as a nitrite reductase to produce nitric oxide during hypoxia. One of the most intriguing aspects of the myoglobin/nitrite interactions revealed so far is the unusual O-binding mode of nitrite to the ferric heme iron, although conflicting data have been reported for the electronic structure of this complex also raising the possibility of linkage isomerism. In this work, we applied resonance Raman spectroscopy in a temperature-dependent approach to investigate the binding of nitrite to ferric myoglobin and the properties of the formed adduct from ambient to low temperatures (293 K to 153 K).