Results 31 to 40 of about 9,153 (190)
Chaperone-Assisted Soluble Expression of a Humanized Anti-EGFR ScFv Antibody in E. Coli [PDF]
Advanced Pharmaceutical Bulletin, 2015 Purpose: Formation of inclusion bodies is a considerable obstacle threatening the advantages of E. coli expression system to serve as the most common and easiest system in recombinant protein production.
Kamal Veisi +6 more
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Foods, 2022 Indigo is an important pigment widely used in industries of food, cosmetics, and textile. In this work, the styrene monooxygenase StyAB from Pseudomonas putida was co-expressed with the tryptophanase TnaA and the chaperone groES-groEL in Escherichia coli
Lingyan Du +3 more
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Stability of Recombinant Proteins in Escherichia coli: The Effect of Co-Expression of Five Different Chaperone Sets [PDF]
Journal of Sciences, Islamic Republic of Iran, 2009 Chaperones are produced by prokaryotic, yeast and higher eukaryotic cells for various purposes. Over-expression of each chaperone or sets of them affect the production level of a recombinant protein in the cell.
H. Mirzahoseini
doaj
Tissue MicroArray (TMA) analysis of normal and persistent
BMC Infectious Diseases, 2006 Background Chlamydophila pneumoniae infection has been implicated as a potential risk factor for atherosclerosis, however the mechanism leading to persistent infection and its role in the disease process remains to be elucidated. Methods We validated the
Timms Peter +8 more
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Emerging themes in the Identifying Successful STARTS Methodologies project and exhibition
Artnodes, 2023 In 2019 a team of multi-disciplinary researchers undertook a research project entitled Identifying Successful STARTS Methodologies (ISSM) (2019-2021) in order to analyze the innovative and collaborative strategies utilized by the global Science ...
Denise Doyle +3 more
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Microorganisms, 2022 The biodegradable polyester poly-(R)-3-hydroxybutyrate [P(3HB)] is synthesized by a polymerizing enzyme called polyhydroxyalkanoate (PHA) synthase and accumulates in a wide variety of bacterial cells. Recently, we demonstrated the secretory production of
Saki Goto +4 more
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Streptomyces lividans groES, groEL1 and groEL2 genes [PDF]
Microbiology, 1997 The Streptomyces lividans groES/ELI operon and groEL2 gene were cloned and their respective DNA sequences determined. The sequenced DNA comprised the genes and their respective regulatory regions in both cases. Transcription of both groES/EL1 and groEL2 seemed to be subjected to temporal control at 30 °C.
Patricia, de León +5 more
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Bridging between NMA and Elastic Network Models: Preserving All-Atom Accuracy in Coarse-Grained Models. [PDF]
PLoS Computational Biology, 2015 Dynamics can provide deep insights into the functional mechanisms of proteins and protein complexes. For large protein complexes such as GroEL/GroES with more than 8,000 residues, obtaining a fine-grained all-atom description of its normal mode motions ...
Hyuntae Na +2 more
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Limits of Protein Folding Inside GroE Complexes [PDF]
Journal of Biological Chemistry, 2000 The GroE chaperones of Escherichia coli promote the folding of other proteins under conditions where no spontaneous folding occurs. One requirement for this reaction is the trapping of the nonnative protein inside the chaperone complex. Encapsulation may be important to prevent unfavorable intermolecular interactions during folding.
H, Grallert, K, Rutkat, J, Buchner
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Friends in need: How chaperonins recognize and remodel proteins that require folding assistance
Frontiers in Molecular Biosciences, 2022 Chaperonins are biological nanomachines that help newly translated proteins to fold by rescuing them from kinetically trapped misfolded states. Protein folding assistance by the chaperonin machinery is obligatory in vivo for a subset of proteins in the ...
George Stan +3 more
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