AbstractCo-expression of the two genes encoding the α- and β-subunit of the Thermoplasma acidophilum thermosome in Escherichia coli yielded fully assembled hetero-oligomeric complexes (α + β). Surprisingly, also separate expression of both genes resulted in formation of hexadecameric complexes (α, β) in the bacterial cytoplasm. On electron micrographs these complexes were indistinguishable from each other and from the native thermosome. The recombinant a-complex as well as the native thermosome could be reconstituted in vitro from their dissociated subunits in the presence of Mg-ATP
The archaeon Methanopyrus kandleri is the most thermophilic methanogen presently known. It contains ...
Tesis Doctoral inédita leída en la Universidad Autónoma de Madrid, Facultad de Ciencias, Departament...
Chaperonins are ubiquitous multi-subunit macromolecules that mediate the folding and assembly of cer...
AbstractCo-expression of the two genes encoding the α- and β-subunit of the Thermoplasma acidophilum...
Go-expression of the two genes encoding the alpha- and beta-subunit of the Thermoplasma acidophilum ...
The thermosome of the archaeon Thermoplasma acidophilum is composed of two subunits, alpha and beta,...
Recent structural data imply differences in allosteric behavior of the group I chaperonins, typified...
Recent structural data imply differences in allosteric behavior of the group I chaperonins, typified...
AbstractThe thermosome, the chaperonin of the archaea, and its homologue from the cytosol of eukaryo...
AbstractWe have determined to 2.6 Å resolution the crystal structure of the thermosome, the archaeal...
A high molecular-mass protein complex from the archaebacterium Thermoplasma acidophilum, referred to...
AbstractThe crystal structure of the substrate binding domain of the thermosome, the archaeal group ...
Chaperonins are double-ring protein folding machines fueled by ATP binding and hydrolysis. Conformat...
AbstractChaperonins are double-ring protein folding machines fueled by ATP binding and hydrolysis. C...
Chaperonins are ubiquitous multi-subunit macromolecules that mediate the folding and assembly of cer...
The archaeon Methanopyrus kandleri is the most thermophilic methanogen presently known. It contains ...
Tesis Doctoral inédita leída en la Universidad Autónoma de Madrid, Facultad de Ciencias, Departament...
Chaperonins are ubiquitous multi-subunit macromolecules that mediate the folding and assembly of cer...
AbstractCo-expression of the two genes encoding the α- and β-subunit of the Thermoplasma acidophilum...
Go-expression of the two genes encoding the alpha- and beta-subunit of the Thermoplasma acidophilum ...
The thermosome of the archaeon Thermoplasma acidophilum is composed of two subunits, alpha and beta,...
Recent structural data imply differences in allosteric behavior of the group I chaperonins, typified...
Recent structural data imply differences in allosteric behavior of the group I chaperonins, typified...
AbstractThe thermosome, the chaperonin of the archaea, and its homologue from the cytosol of eukaryo...
AbstractWe have determined to 2.6 Å resolution the crystal structure of the thermosome, the archaeal...
A high molecular-mass protein complex from the archaebacterium Thermoplasma acidophilum, referred to...
AbstractThe crystal structure of the substrate binding domain of the thermosome, the archaeal group ...
Chaperonins are double-ring protein folding machines fueled by ATP binding and hydrolysis. Conformat...
AbstractChaperonins are double-ring protein folding machines fueled by ATP binding and hydrolysis. C...
Chaperonins are ubiquitous multi-subunit macromolecules that mediate the folding and assembly of cer...
The archaeon Methanopyrus kandleri is the most thermophilic methanogen presently known. It contains ...
Tesis Doctoral inédita leída en la Universidad Autónoma de Madrid, Facultad de Ciencias, Departament...
Chaperonins are ubiquitous multi-subunit macromolecules that mediate the folding and assembly of cer...