Results 41 to 50 of about 27,570 (293)
Streptomyces lividans groES, groEL1 and groEL2 genes [PDF]
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]
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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The Proteome of Biologically Active Membrane Vesicles from Piscirickettsia salmonis LF-89 Type Strain Identifies Plasmid-Encoded Putative Toxins [PDF]
Indexación: Scopus.Piscirickettsia salmonis is the predominant bacterial pathogen affecting the Chilean salmonid industry. This bacterium is the etiological agent of piscirickettsiosis, a significant fish disease.
Artigues, A. +14 more
core +1 more source
Hegemonic and Subordinated Masculinities
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
doaj +1 more source
Molecular Mechanisms of Chaperonin GroEL−GroES Function [PDF]
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
openaire +2 more sources
Chaperone-Assisted Soluble Expression of a Humanized Anti-EGFR ScFv Antibody in E. Coli [PDF]
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
doaj +1 more source
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
doaj +1 more source
Tissue MicroArray (TMA) analysis of normal and persistent
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
doaj +1 more source
Hsp70 in mitochondrial biogenesis [PDF]
The family of hsp70 (70 kilodalton heat shock protein) molecular chaperones plays an essential and diverse role in cellular physiology, Hsp70 proteins appear to elicit their effects by interacting with polypeptides that present domains which exhibit non ...
A. Tzagoloff +53 more
core +1 more source
Stability of Recombinant Proteins in Escherichia coli: The Effect of Co-Expression of Five Different Chaperone Sets [PDF]
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

