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Showing 1 to 12 of 12 for “"chaperonins"”.
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Functional and structural characterisation of Mycobacterial Chaperonins
… are 2 distinct groEL homologues which encode the chaperonins Cpn60.1 and Cpn60.2, with the latter predicted to be the main house-keeping chaperonin. Phylogenetic analysis has revealed that the genes for the duplicated chaperonins diverged a long time ago. This implies that the duplicated …
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Analysis of the multiple chaperonins of Mycobacterium smegmatis
… study is a functional characterisation of the chaperonins of M. smegmatis. Expression of cpn60.1, cpn60.2 and cpn10, but not cpn60.3, was found to be induced under stress conditions, particularly heat shock. Studies of the cpn10-cpn60.1 operon concluded that transcription is from a single …
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Function and Properties of groE Chaperonins in Bacterial and Mammalian Cells
… best characterized of the ringed chaperones, or chaperonins. Chaperonins of the eukaryotic cytoplasm interact with a limited number of polypeptides, whereas GroEL is promiscuous as it binds and mediates the folding of many polypeptides. This feature makes GroEL an attractive protein for …
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Elucidating aquatic virioplankton diversity and dynamics using high-throughput DNA sequencing
… involved in nucleotide and protein metabolism. Chaperonins, a conserved protein-folding system found in all cellular life, were explored in viral metagenomic data. Contrary to the low frequency of chaperonin-encoding viruses in sequence databases, a surprising diversity and abundance of viral …
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Role of Chaperonin CCT in G-protein Biosynthesis
Chaperonins are ubiquitous molecular chaperones that are found in all animal kingdoms. They all share a common structure and function to assist the folding of other proteins. All chaperonins consist of two stacked rings, which come together to form a central cavity where folding can take place. The …
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Assembly and substrate recognition properties of human CCT subunits of the TRiC chaperonin
Group II chaperonins are large multi-subunit complexes that fold cytosolic proteins to their native structures. They are composed of two back-to-back rings of 7-9 subunits. The eukaryotic cytosolic type II chaperonin Tailless Complex Polypeptide-1 (TCP-1) Ring Complex (TRiC) consists of eight …
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Allostery and GroEL: Exploring the Tenets of Nested Cooperativity
… on the functional cycle of the <i>E. coli</i> chaperonins GroEL and GroES, no model proposed to date accounts for all the effects seen experimentally by the various allosteric ligands: ATP, ADP, SP, GroES, and K+. The work in this dissertation explores the various allosteric transitions in the …
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Relationships Between Expression of Heat Shock Protein Genes and Photosynthetic Behavior During Drought Stress in Plants
… correlated with up-regulation of HSPs (mostly chaperonins) and antioxidant genes all of whose gene products are located in the chloroplast.
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Identification and Characterization of Aer, an Energy Sensor in Escherichia Coli
… inclusion bodies. Co-expressing the GroESL chaperonins alleviated inclusion body formation and increased the solubility of Aer.</p>
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Design of Single-Chain Polymer Nanoparticles to Mimic Globular Proteins
… can function as catalysts, proton channels, and chaperonins. By comparing the behaviors of MMA-based RHPs with that of globular proteins, I provide fundamental physicochemical insights and design principles for SCNPs as protein mimetics and stabilizers. I highlight the significance of chemical …
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Assessment of the Expression of Brucella Abortus Heat Shock Protein, Groel, in Vaccinia Virus to Induce Protection Against a Brucella Challenge in Balb/C Mice
B. abortus is an intracellular facultative bacterial pathogen which causes abortion in cattle and undulant fever in humans. Cattle vaccines such as B. abortus strains 19 and RB51 are live vaccine strains which protect approximately 75% of the vaccinated animals. No effective vaccines are available …
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Untersuchung der Reaktionszyklen von Chaperoninen aus Escherichia coli und Thermoplasma acidophilum mit Hilfe der Neutronenkleinwinkelstreuung
… im strukturellen Reaktionszyklus des Chaperonins charakterisiert werden. - Bei einer Reihe von Pufferbedingungen wurde die Bildung von Komplexen höherer Ordnung beobachtet. Von anderen Autoren war aufgrund von EM-Arbeiten vorgeschlagen worden, daß Thermosom kein Chaperonin, sondern ein …