190 research outputs found
Bioethanol Production:Characterisation of a Bifunctional Alcohol Dehydrogenase from <em>Geobacillus thermoglucosidasius</em>
Towards Large-Scale Quantum Networks
The vision of a quantum internet is to fundamentally enhance Internet
technology by enabling quantum communication between any two points on Earth.
While the first realisations of small scale quantum networks are expected in
the near future, scaling such networks presents immense challenges to physics,
computer science and engineering. Here, we provide a gentle introduction to
quantum networking targeted at computer scientists, and survey the state of the
art. We proceed to discuss key challenges for computer science in order to make
such networks a reality.Comment: To be presented at the Sixth Annual ACM International Conference on
Nanoscale Computing and Communication, Dublin, Irelan
Structure of an acetylating aldehyde dehydrogenase from the thermophilic ethanologen Geobacillus thermoglucosidasius
Acetylating aldehyde dehydrogenases (AcAldDH) catalyse the acetylation of CoenzymeāA (CoA), or in reverse generate acetaldehyde from AcetylāCoA using NADH as a coāfactor. This article reports the expression, purification, enzyme assay, and Xāray crystal structures of an AcAldDH from Geobacillus thermoglucosidasius (GtAcAldDH) to 2.1Ć
and in complex with CoA and NAD(+) to 4.0Ć
. In the structure, the AcAldDH forms a closeāknit dimer, similar to that seen in other Alcohol Dehydrogenase (ADH) structures. In GtAcAldDH, these dimers associate via their Nātermini to form weakly interacting tetramers. This mode of tetrameric association is also seen in an unpublished AcAldDH deposited in the PDB, but is in contrast to all other ADH structures, (including the one other published AcAldDH found in a bacterial microcompartment), in which the dimers bury a large surface area including the Cātermini. This novel mode of association sequesters the active sites and potentially reactive acylāenzyme intermediates in the center of the tetramer. In other respects, the structure is very similar to the other AcAldDH, binding the cofactors in a corresponding fashion. This similarity enabled the identification of a shortened substrate cavity in G. thermoglucosidasius AcAldDH, explaining the limitations on the length of substrate accepted by the enzyme
Structure of a bifunctional alcohol dehydrogenase involved in bioethanol generation in <em>Geobacillus thermoglucosidasius </em>
Bifunctional alcohol/aldehyde dehydrogenase (ADHE) enzymes are found within many fermentative microorganisms. They catalyse the conversion of an acyl-coenzyme A to an alcoholviaan aldehyde intermediate; this is coupled to the oxidation of two NADH molecules to maintain the NAD+pool during fermentative metabolism. The structure of the alcohol dehydrogenase (ADH) domain of an ADHE protein from the ethanol-producing thermophileGeobacillus thermoglucosidasiushas been determined to 2.5ā
Ć
resolution. This is the first structure to be reported for such a domain.In silicomodelling has been carried out to generate a homology model of the aldehyde dehydrogenase domain, and this was subsequently docked with the ADH-domain structure to model the structure of the complete ADHE protein. This model suggests, for the first time, a structural mechanism for the formation of the large multimeric assemblies or `spirosomes' that are observed for this ADHE protein and which have previously been reported for ADHEs from other organisms.</jats:p
High-density information storage in an absolutely defined aperiodic sequence of monodisperse copolyester
Synthesis of a polymer composed of a large discrete number of chemically distinct monomers in an absolutely defined aperiodic sequence remains a challenge in polymer chemistry. The synthesis has largely been limited to oligomers having a limited number of repeating units due to the difficulties associated with the step-by-step addition of individual monomers to achieve high molecular weights. Here we report the copolymers of ??-hydroxy acids, poly(phenyllactic-co-lactic acid) (PcL) built via the cross-convergent method from four dyads of monomers as constituent units. Our proposed method allows scalable synthesis of sequence-defined PcL in a minimal number of coupling steps from reagents in stoichiometric amounts. Digital information can be stored in an aperiodic sequence of PcL, which can be fully retrieved as binary code by mass spectrometry sequencing. The information storage density (bit/Da) of PcL is 50% higher than DNA, and the storage capacity of PcL can also be increased by adjusting the molecular weight (~38???kDa)
Metabolic engineering of Clostridium autoethanogenum for selective alcohol production
Gas fermentation using acetogenic bacteria such as Clostridium autoethanogenum offers an attractive route for production of fuel ethanol from industrial waste gases. Acetate reduction to acetaldehyde and further to ethanol via an aldehyde: ferredoxin oxidoreductase (AOR) and alcohol dehydrogenase has been postulated alongside the classic pathway of ethanol formation via a bi-functional aldehyde/alcohol dehydrogenase (AdhE). Here we demonstrate that AOR is critical to ethanol formation in acetogens and inactivation of AdhE led to consistently enhanced autotrophic ethanol production (up to 180%). Using ClosTron and allelic exchange mutagenesis, which was demonstrated for the first time in an acetogen, we generated single mutants as well as double mutants for both aor and adhE isoforms to confirm the role of each gene. The aor1+2 double knockout strain lost the ability to convert exogenous acetate, propionate and butyrate into the corresponding alcohols, further highlighting the role of these enzymes in catalyzing the thermodynamically unfavourable reduction of carboxylic acids into alcohols
Data science for the scientific life cycle.
Data science can be incorporated into every stage of a scientific study. Here we describe how data science can be used to generate hypotheses, to design experiments, to perform experiments, and to analyse data. We also present our vision for how data science techniques will be an integral part of the laboratory of the future
Macrocyclic Ī²-Sheet Peptides That Inhibit the Aggregation of a Tau-Protein-Derived Hexapeptide
This paper describes studies of a series of macrocyclic Ī²-sheet peptides 1 that inhibit the aggregation of a tau-protein-derived peptide. The macrocyclic Ī²-sheet peptides comprise a pentapeptide "upper" strand, two Ī“-linked ornithine turn units, and a "lower" strand comprising two additional residues and the Ī²-sheet peptidomimetic template "Hao". The tau-derived peptide Ac-VQIVYK-NH(2) (AcPHF6) aggregates in solution through Ī²-sheet interactions to form straight and twisted filaments similar to those formed by tau protein in Alzheimer's neurofibrillary tangles. Macrocycles 1 containing the pentapeptide VQIVY in the "upper" strand delay and suppress the onset of aggregation of the AcPHF6 peptide. Inhibition is particularly pronounced in macrocycles 1a, 1d, and 1f, in which the two residues in the "lower" strand provide a pattern of hydrophobicity and hydrophilicity that matches that of the pentapeptide "upper" strand. Inhibition varies strongly with the concentration of these macrocycles, suggesting that it is cooperative. Macrocycle 1b containing the pentapeptide QIVYK shows little inhibition, suggesting the possibility of a preferred direction of growth of AcPHF6 Ī²-sheets. On the basis of these studies, a model is proposed in which the AcPHF6 amyloid grows as a layered pair of Ī²-sheets and in which growth is blocked by a pair of macrocycles that cap the growing paired hydrogen-bonding edges. This model provides a provocative and appealing target for future inhibitor design
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