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The crystal structure of glucose dehydrogenase from Thermoplasma acidophilum [PDF]

open access: yesStructure, 1994
The archaea are a group of organisms distinct from bacteria and eukaryotes. Structures of proteins from archaea are of interest because they function in extreme environments and because structural studies may reveal evolutionary relationships between proteins.
Susan Crennell   +2 more
exaly   +3 more sources
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Proteasome from Thermoplasma acidophilum : a Threonine Protease

Science, 1995
The catalytic mechanism of the 20 S proteasome from the archaebacterium Thermoplasma acidophilum has been analyzed by site-directed mutagenesis of the β subunit and by inhibitor studies. Deletion of the amino-terminal threonine or its mutation to alanine led to inactivation of the enzyme ...
Seemüller, E.   +5 more
openaire   +7 more sources

The Chaperones of the Archaeon Thermoplasma acidophilum

Journal of Structural Biology, 2001
Chaperonesare an essential component of a cell's ability to respond to environmental challenges. Chaperones have been studied primarily in bacteria, but in recent years it has become apparent that some classes of chaperones either are very divergent in bacteria relative to archaea and eukaryotes or are missing entirely.
Ruepp, A.   +4 more
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Glucosylcaldarchaetidylglycerol, a minor phosphoglycolipid from Thermoplasma acidophilum

Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids, 2000
A novel phosphoglycolipid (GPL-K) was isolated from Thermoplasma acidophilum (ATCC 27658). The chemical components of GPL-K were analyzed by gas liquid chromatography and GC-MS. The sugar moiety of GPL-K and its anomeric region were analyzed by NMR assignment.
I, Uda   +4 more
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A new class of lipopolysaccharide from Thermoplasma acidophilum

Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1974
Abstract A hot aqueous phenol extraction of lipid extracted whole cells of Thermoplasma acidophilum yielded a polymer that comprises 97% of the aqueous phase. The polymer is composed of 80% carbohydrate and 20% glycerol diether. Analysis of this polymer showed a ratio of 25:1:2 of carbohydrate: glycerol: alkane.
K J, Mayberry-Carson   +3 more
openaire   +2 more sources

Primary Structure of the Thermosome fromThermoplasma acidophilum

Biological Chemistry Hoppe-Seyler, 1995
The thermosome, a chaperonin from the archaebacterium Thermoplasma acidophilum, consists of two subunits (M(r) 58,000 and 60,000) which assemble into a cylindrical complex of pseudo eight-fold rotational symmetry. The sequences of the two subunits are approximately 60% identical to each other and to TF55 from Sulfolobus shibatae, and are 30-40 ...
Waldmann, T.   +4 more
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Superoxide dismutase from the archaebacterium Thermoplasma acidophilum

Biochimica et Biophysica Acta (BBA) - Protein Structure, 1981
Thermoplasma acidophilum is a mycoplasma-like thermophilic organism that has been classified with the archaebacteria. It has a single superoxide dismutase (superoxide : superoxide oxidoreductase, EC 1.15.1.1) which is composed of four identically sized subunits.
K B, Searcy, D G, Searcy
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Biochemical properties of the proteasome from Thermoplasma acidophilum

European Journal of Biochemistry, 1992
We have purified proteasomes to apparent homogeneity from the archaebacterium Thermoplasma acidophilum. This proteinase has a molecular mass of about 650 kDa and an isoelectric point of 5.6. The proteasome hydrolyses peptide substrates containing an aromatic residue adjacent to the reporter group, as well as [14C]methylated casein optimally at pH 8.5 ...
Dahlmann, B.   +4 more
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Thermoplasma acidophilum: Intracellular pH and potassium concentration

Biochimica et Biophysica Acta (BBA) - General Subjects, 1976
Thermoplasma acidophilum is a free-living thermophilic mycoplasma. Although the organism lacks a cell wall, it can grow in medium as dilute as 66 mosM. The intracellular K+ concentration can be as low as 17 mM, but varies according to the osmolality of the culture medium.
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