8 results match your criteria: "Institute of Biological Instrumentation[Affiliation]"
Lett Appl Microbiol
December 2024
The Institute of Biological Instrumentation of the Russian Academy of Sciences (IBI RAS), Federal Research Center Pushchino Scientific Center for Biological Research of the Russian Academy of Sciences (PSCBR RAS), Institutskaya 7, Pushchino, Moscow Region 142290, Russia.
Basidiomycetes, known for their production of bioactive compounds, traditionally use simple sugars for fermentation. However, their ability to degrade complex plant polysaccharides through enzyme secretion presents potential for the use of renewable raw materials. This study focused on the optimization of exopolysaccharide (EPS) production and efficient substrate consumption by Ganoderma lucidum using response surface methodology (RSM).
View Article and Find Full Text PDFMol Biol (Mosk)
October 2021
Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow oblast, 142290 Russia.
The review summarizes and systematizes the data on the classification, taxonomic distribution, structural features, and functions of proteins with structural repeats. Modern approaches to the identification of structural repeats in proteins are considered. Features of specialized databases of protein domains are described.
View Article and Find Full Text PDFProg Mol Biol Transl Sci
November 2021
G.B. Elyakov Pacific Institute of Bioorganic Chemistry, Far East Branch, Russian Academy of Sciences, Vladivostok, Russia.
Features of the structure and functional activity of bacterial outer membrane porins, coupled with their dynamic "behavior," suggests that intrinsically disordered regions (IDPRs) are contained in their structure. Using bioinformatic analysis, the quantitative content of amyloidogenic regions in the amino acid sequence of non-specific porins inhabiting various natural niches was determined: from terrestrial bacteria of the genus Yersinia (OmpF and OmpC proteins of Y. pseudotuberculosis and Y.
View Article and Find Full Text PDFIntrinsically Disord Proteins
March 2017
Department of Molecular Medicine, Morsani College of Medicine, University of South Florida, Tampa, FL, USA; USF Health Byrd Alzheimer's Research Institute, Morsani College of Medicine, University of South Florida, Tampa, FL, USA; Laboratory of New Methods in Biology, Institute of Biological Instrumentation, Russian Academy of Sciences, Pushchino, Moscow Region, Russia; Laboratory of Structural Dynamics, Stability and Folding of Proteins, Institute of Cytology, Russian Academy of Sciences, St. Petersburg, Russia.
This is the 6 issue of the Digested Disorder series that continues to use only 2 criteria for inclusion of a paper to this digest: The publication date (a paper should be published within the covered time frame) and the topic (a paper should be dedicated to any aspect of protein intrinsic disorder). The current digest issue covers papers published during the second quarter of 2014; i.e.
View Article and Find Full Text PDFBioorg Khim
July 2002
Institute of Biological Instrumentation, Russian Academy of Sciences, Pushchino, Moscow Oblast, 142290 Russia.
The kinetics of the reaction of Boc-Xaa fluorophenyl esters (where Xaa = Ala, Val, Phe, Ser, Leu, Gly, Met, Pro, or Ile) with leucinamide was studied measuring changes in the fluorescence emission at 375 nm of the fluorophenyl chromophore accompanying the reaction. It was found that the experimental kinetic data couldn't be described by a simple scheme of the second order reaction. The measurements of the kinetic parameters of the reaction at various initial concentrations of reagents indicated that the reaction rate can be expressed as: v = kCNaCAEb, where k is the reaction rate constant, CN is the concentration of leucinamide, and LeuNH2, CAE is the concentration of fluorophenyl ester.
View Article and Find Full Text PDFBiochemistry (Mosc)
December 2001
Institute of Biological Instrumentation, Russian Academy of Sciences, Pushchino, Moscow Region, 142292 Russia.
Covalently cross-linked rod-like dimers of human myeloma IgG3 are more efficient in the inhibition of the complement system reaction than compact dimers. This correlates with an increase in the stability of CH2 domains of the immunoglobulin in the state with the rod-like hinge region.
View Article and Find Full Text PDFBiofizika
February 2001
Institute of Biological Instrumentation, Russian Academy of Sciences, Pushchino, Moscow Region, 142290 Russia.
Major results of the use of protein engineering methods in studies of calcium-binding proteins with the highest affinity for calcium and known three-dimensional structure (parvalbumin, calmodulin, troponin C, calbindin, recoverin, alpha-lactalbumin, and others) are presented. Specific features of recombinant calcium-binding proteins are discussed. Experiments with genetic introduction of fluorescent probes, tryptophan and tyrosine, into proteins are overviewed.
View Article and Find Full Text PDFBiochemistry (Mosc)
October 2000
Institute of Biological Instrumentation, Russian Academy of Sciences, Pushchino, Moscow Region, 142292, Russia.
The structure of the pFh-fragment (hinge region) from human myeloma IgG3 Kuc (the third subclass immunoglobulin) was studied by hydrodynamic methods in the pH range from 3.0 to 8.0.
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