Results 31 to 40 of about 23,956 (223)
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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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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Hegemonic and Subordinated Masculinities
Nordic Journal of African Studies, 2009 The article explores theoretical implications of sexual and violent practices among disenfranchised young men in Southern Africa. Ethnographic findings from Maputo, Mozambique indicate that massive unemployment caused by neo-liberal reforms have led to ...
Christian Groes-Green
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Molecular Mechanisms of Chaperonin GroEL−GroES Function [PDF]
Biochemistry, 2001 The dynamics of the GroEL-GroES complex is investigated with a coarse-grained model. This model is one in which single-residue points are connected to other such points, which are nearby, by identical springs, forming a network of interactions. The nature of the most important (slowest) normal modes reveals a wide variety of motions uniquely dependent ...
O, Keskin +4 more
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An integrated native mass spectrometry and top-down proteomics method that connects sequence to structure and function of macromolecular complexes. [PDF]
, 2018 Mass spectrometry (MS) has become a crucial technique for the analysis of protein complexes. Native MS has traditionally examined protein subunit arrangements, while proteomics MS has focused on sequence identification.
Campuzano, Iain DG +4 more
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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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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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An Adaptation To Life In Acid Through A Novel Mevalonate Pathway. [PDF]
, 2016 Extreme acidophiles are capable of growth at pH values near zero. Sustaining life in acidic environments requires extensive adaptations of membranes, proton pumps, and DNA repair mechanisms.
Bowie, James U +3 more
core +1 more source
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
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