Results 51 to 60 of about 1,932 (141)
Domain swapping: a mathematical model for quantitative assessment of structural effects
FEBS Open Bio, Volume 14, Issue 12, Page 2006-2025, December 2024.The structure of a single chain interpreted on the basis of the hydrophobicity distribution (red line on profiles) represents the status with respect to an ideal hydrophobic core (blue) which is represented by a modified idealised hydrophobicity distribution (green line, upper part).
Irena Roterman +3 more
wiley +1 more source
Metal ion activation and DNA recognition by the Deinococcus radiodurans manganese sensor DR2539
The FEBS Journal, Volume 291, Issue 15, Page 3384-3402, August 2024.The manganese sensor DR2539 from Deinococus radiodurans recognises the dr1709 promoter region, which consists of a 21 base pair pseudo‐palindrome binding two DR2539 monomers. Here, we identified four manganese binding sites and investigated protein‐DNA interactions, with critical nucleotides being probed.
Cristiano Mota +7 more
wiley +1 more source
ChemSusChem, Volume 17, Issue 4, February 22, 2024.This work demonstrates the power of enzyme engineering to tailor a biocatalyst to meet various requirements of a cell‐free artificial multi‐enzyme cascade. We targeted glyceraldehyde dehydrogenase (GADH) as a key enzyme to efficiently produce ethanol from D‐glucose (obtainable from lignocellulosic agricultural wastes).
Mariko Teshima +6 more
wiley +1 more source
ChemBioChem, Volume 25, Issue 1, January 2, 2024.A ferredoxin from Archaeoglobus fulgidus has been identified that regenerates the cofactor in the corresponding geranylgeranyl reductase (GGR) for the reduction of isolated C=C bonds. The reaction was coupled to an unspecific ferredoxin reductase from E.
Richard Niese +2 more
wiley +1 more source
The FEBS Journal, Volume 291, Issue 1, Page 177-203, January 2024.Invasion of brain endothelium protein A (IbeA), a virulence factor specific to pathogenic Escherichia coli, plays an important role in the invasion of host cells by the intestinal adherent invasive Escherichia coli strain involved in Crohn's disease and in the survival of these bacteria within host macrophages.
Théo Paris +7 more
wiley +1 more source
Ultrastructural localization of Thermoplasma acidophilum surface carbohydrate by using concanavalin A [PDF]
Journal of Bacteriology, 1978 Surface carbohydrate, presumably the lipopolysaccharide, of Thermoplasma acidophilum was visualized by means of the concanavalin A, horseradish peroxidase, and diaminobenzidine cytochemical staining procedure.
K J, Mayberry-Carson +2 more
openaire +2 more sources
Archaea, Volume 2024, Issue 1, 2024.Archaeal species encode a diversity of chromatin proteins that play distinct roles in genome compaction. Although our understanding of the individual proteins has been growing, their contributions to higher‐order folding in the archaeal chromosome remain to be explored. In this study, we investigated the chromatin structure of Thermoplasma volcanium, a
Kirk Amerigo B. Aycardo +2 more
wiley +1 more source
Physicochemical Characterization of Tetraetherlipids from Thermoplasma acidophilum
Zeitschrift für Naturforschung C, 1985 Abstract By means of differential thermoanalysis, the miscibility of the main polar tetraether lipid of Thermoplasma acidophilum with two ester lipids, dipalmitoyl phosphatidylcholine and dipalmitoyl phosphatidylglycerol, resp., in the presence of excess water was studied. It is shown that with increasing fraction of tetraether lipid in
Blöcher, Detlef +3 more
openaire +2 more sources
Organization of rRNA structural genes in the archaebacteriumThermoplasma acidophilum
Nucleic Acids Research, 1982 In the archaebacterium Thermoplasma acidophilum, each of the structural genes for 5S, 16S and 23S rRNA occur once per genome. In contrast to those of eubacteria and eukaryotes, they appear unlinked. The distance between the 16S and the 23S rDNA is at least 7.5 Kb, that between 23S and 5S rDNA at least 6 Kb and that between 16S and 5S rDNA at least 1.5 ...
J, Tu, W, Zillig
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Expression of functional Thermoplasma acidophilum proteasomes in Escherichia coli
FEBS Letters, 1992 The two genes encoding the constituent subunits of the Thermoplasma acidophilum proteasome were expressed in Escherichia coli yielding fully assembled molecules as shown by electron microscopy. The recombinant proteasomes were purified to homogeneity and ware shown to have proteolytic activity indistinguishable from proteasomes isolated from T ...
Zwickl, P. +2 more
openaire +3 more sources