17 research outputs found
EXPERIENCE OF ORGANIZING TRAINING OF PROFESSIONALS FOR HIGH-TECH INDUSTRIES
The article describes some approaches to the organization of training of professionals for high-tech industries at the UNN Faculty of Physics using the resources of the Physical-Technical Research Institute of UNN. The paper presents a number of successful results of this activity. It is shown that the combination of fundamental training carried out at the classical Faculty of Physics and practical training at the Research Institute focused on the application of research results in the industry ensures a new level of quality for the competences of the University graduates
Method for Identification of Threonine Isoforms in Peptides by Ultraviolet Photofragmentation of Cold Ions
Identification of isomeric amino acid residues in peptides and proteins is challenging but often highly desired in proteomics. One of the practically important cases that require isomeric assignments is that associated with single-nucleotide polymorphism substitutions of Met residues by Thr in cancer-related proteins. These genetically encoded substitutions can yet be confused with the chemical modifications, arising from protein alkylation by iodoacetamide, which is commonly used in the standard procedure of sample preparation for proteomic analysis. Similar to the genetically encoded mutations, the alkylation also induces a conversion of methionine residues, but to the iso-threonine form. Recognition of the mutations therefore requires isoform-sensitive detection techniques. Herein, we demonstrate an analytical method for reliable identification of isoforms of threonine residues in tryptic peptides. It is based on ultraviolet photodissociation mass spectrometry of cryogenically cooled ions and a machine-learning algorithm. The measured photodissociation mass spectra exhibit isoform-specific patterns, which are independent of the residues adjacent to threonine or iso-threonine in a peptide sequence. A comprehensive metric-based evaluation demonstrates that, being calibrated with a set of model peptides, the method allows for isomeric identification of threonine residues in peptides of arbitrary sequence
Extracellular Membrane Vesicles and Phytopathogenicity of Acholeplasma laidlawii PG8
For the first time, the phytopathogenicity of extracellular vesicles of Acholeplasma laidlawii PG8 (a ubiquitous mycoplasma that is one of the five common species of cell culture contaminants and is a causative agent for phytomycoplasmoses) in Oryza sativa L. plants was studied. Data on the ability of extracellular vesicles of Acholeplasma laidlawii PG8 to penetrate from the nutrient medium into overground parts of Oryza sativa L. through the root system and to cause alterations in ultrastructural organization of the plants were presented. As a result of the analysis of ultrathin leaf sections of plants grown in medium with A. laidlawii PG8 vesicles, we detected significant changes in tissue ultrastructure characteristic to oxidative stress in plants as well as their cultivation along with bacterial cells. The presence of nucleotide sequences of some mycoplasma genes within extracellular vesicles of Acholeplasma laidlawii PG8 allowed a possibility to use PCR (with the following sequencing) to perform differential detection of cells and bacterial vesicles in samples under study. The obtained data may suggest the ability of extracellular vesicles of the mycoplasma to display in plants the features of infection from the viewpoint of virulence criteriaâinvasivity, infectivityâand toxigenicityâand to favor to bacterial phytopathogenicity
Atmospheric Pressure Ionization Permanent Magnet Fourier Transform Ion Cyclotron Resonance Mass Spectrometry
A new Fourier transform ion cyclotron resonance mass spectrometer based on a permanent magnet with an atmospheric pressure ionization source was designed and constructed. A mass resolving power (full-width-at-half-maximum) of up to 80,000 in the electron ionization mode and 25,000 in the electrospray mode was obtained. Also, a mass measurement accuracy at low-ppm level has been demonstrated for peptide mixtures in a mass range of up to 1200 m/z in the isotopically resolved mass spectra