295 research outputs found

    The Rock Cycle

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    Grade Level(s): 4-8Edmunds Central School, Roscoe, S

    La gestion de projet croise le wiki

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    La complexité est au premier rang des défis en gestion de projet. Un outil de collaboration issu des technologies du Web 2.0 appelé "wiki" offre de nouvelles pistes de réponses à cette problématique. L'objectif principal de cette recherche est de montrer comment le wiki peut nous aider à composer avec la complexité en gestion de projet. Plus précisément, il s'agit de s'appuyer sur les tremplins de la systémique et de la complexité pour proposer une modélisation du système wiki avant de tenter de le légitimer à partir de données recueillies sur le terrain. Pour ce faire, une étude de cas a été réalisée sur une période de cinq mois auprès d'une entreprise oeuvrant dans le secteur des télécommunications. Celle-ci a mis en place un wiki pilote pour servir de plateforme de collaboration au développement d'un logiciel de test interne. Cette recherche constructiviste, suit une approche exploratoire. Son cadre conceptuel se fonde sur une revue des notions théoriques dans les domaines de la systémique, de la complexité et du wiki. Sont explorés notamment les trois principes morinniens de la dialogique, de la récursion et de l'hologramme. La collecte des données s'est faite à partir d'entrevues préliminaires, d'un sondage intermédiaire, de documents internes et d'une observation directe participative.\ud En définitive, cette recherche devrait apporter des contributions tant conceptuelles que managériales à la problématique de la complexité en gestion de projet. ______________________________________________________________________________ MOTS-CLÉS DE L’AUTEUR : Complexité, Gestion de projet, Systémique, Hologramme, Récursion, Dialogique, Wiki, Technologie, Web 2.0, Collaboration

    Structure of human Fe–S assembly subcomplex reveals unexpected cysteine desulfurase architecture and acyl-ACP–ISD11 interactions

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    In eukaryotes, sulfur is mobilized for incorporation into multiple biosynthetic pathways by a cysteine desulfurase complex that consists of a catalytic subunit (NFS1), LYR protein (ISD11), and acyl carrier protein (ACP). This NFS1-ISD11-ACP (SDA) complex forms the core of the iron-sulfur (Fe-S) assembly complex and associates with assembly proteins ISCU2, frataxin (FXN), and ferredoxin to synthesize Fe-S clusters. Here we present crystallographic and electron microscopic structures of the SDA complex coupled to enzyme kinetic and cell-based studies to provide structure-function properties of a mitochondrial cysteine desulfurase. Unlike prokaryotic cysteine desulfurases, the SDA structure adopts an unexpected architecture in which a pair of ISD11 subunits form the dimeric core of the SDA complex, which clarifies the critical role of ISD11 in eukaryotic assemblies. The different quaternary structure results in an incompletely formed substrate channel and solvent-exposed pyridoxal 5'-phosphate cofactor and provides a rationale for the allosteric activator function of FXN in eukaryotic systems. The structure also reveals the 4'-phosphopantetheine-conjugated acyl-group of ACP occupies the hydrophobic core of ISD11, explaining the basis of ACP stabilization. The unexpected architecture for the SDA complex provides a framework for understanding interactions with acceptor proteins for sulfur-containing biosynthetic pathways, elucidating mechanistic details of eukaryotic F e-S cluster biosynthesis, and clarifying how defects in Fe-S cluster assembly lead to diseases such as Friedreich's ataxia. Moreover, our results support a lock-and-key model in which LYR proteins associate with acyl-ACP as a mechanism for fatty acid biosynthesis to coordinate the expression, Fe-S cofactor maturation, and activity of the respiratory complexes. Keywords: LYR; ACP; iron-sulfur cluster; PLP; frataxi

    Embedding the Ni-SOD mimetic Ni-NCC within a polypeptide sequence alters specificity of the reaction pathway

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    This document is the Accepted Manuscript version of a Published Work that appeared in final form in the Inorganic Chemistry, copyright © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see http://doi.org/10.1021/ic301175f.The unique metal abstracting peptide (MAP) asparagine-cysteine-cysteine (NCC) binds nickel in a square planar 2N:2S geometry and acts as a mimic of the enzyme nickel superoxide dismutase (Ni-SOD). The Ni-NCC tripeptide complex undergoes rapid, site-specific chiral inversion to DLD-NCC in the presence of oxygen. Superoxide scavenging activity increases proportionally with the degree of chiral inversion. Characterization of the NCC sequence within longer peptides with absorption, circular dichroism (CD), and magnetic CD (MCD) spectroscopies and mass spectrometry (MS) shows that the geometry of metal coordination is maintained, though the electronic properties of the complex are varied to a small extent due to bis-amide, rather than amine/amide, coordination. In addition, both the Ni-tripeptides and Ni-pentapeptides have a −2 charge. The study here demonstrates that the chiral inversion chemistry does not occur when NCC is embedded in a longer polypeptide sequence. Nonetheless, the superoxide scavenging reactivity of the embedded Ni-NCC module is similar to that of the chirally inverted tripeptide complex, which is consistent with a minor change in reduction potential for the Ni-pentapeptide. Together, this suggests that the charge of the complex could affect the SOD activity as much as a change in primary coordination sphere. In Ni-NCC and other Ni-SOD mimics, changes in chirality, superoxide scavenging activity, and oxidation of the peptide itself all depend on the presence of dioxygen or its reduced derivatives (e.g., superoxide), and the extent to which each of these distinct reactions occurs is ruled by electronic and steric effects that emenate from the organization of ligands around the metal center

    Biological conversion of carbon monoxide: rich syngas or waste gases to bioethanol

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    Bioconversion of syngas/waste gas components to produce ethanol appears to be a promising alternative compared to the existing chemical techniques. Recently, several laboratory-scale studies have demonstrated the use of acetogens that have the ability to convert various syngas components (CO, CO2, and H2) to multicarbon compounds, such as acetate, butyrate, butanol, lactate, and ethanol, in which ethanol is often produced as a minor end-product. This bioconversion process has several advantages, such as its high specificity, the fact that it does not require a highly specific H2/CO ratio, and that biocatalysts are less susceptible to metal poisoning. Furthermore, this process occurs under mild temperature and pressure and does not require any costly pre-treatment of the feed gas or costly metal catalysts, making the process superior over the conventional chemical catalytic conversion process. The main challenge faced for commercializing this technology is the poor aqueous solubility of the gaseous substrates (mainly CO and H2). In this paper, a critical review of CO-rich gas fermentation to produce ethanol has been analyzed systematically and published results have been compared. Special emphasis has been given to understand the microbial aspects of the conversion process, by highlighting the role of different micro-organisms used, pathways, and parameters affecting the bioconversion. An analysis of the process fundamentals of various bioreactors used for the biological conversion of CO-rich gases, mainly syngas to ethanol, has been made and reported in this paper. Various challenges faced by the syngas fermentation process for commercialization and future research requirements are also discussed

    Design Strategies of Fluorescent Biosensors Based on Biological Macromolecular Receptors

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    Fluorescent biosensors to detect the bona fide events of biologically important molecules in living cells are increasingly demanded in the field of molecular cell biology. Recent advances in the development of fluorescent biosensors have made an outstanding contribution to elucidating not only the roles of individual biomolecules, but also the dynamic intracellular relationships between these molecules. However, rational design strategies of fluorescent biosensors are not as mature as they look. An insatiable request for the establishment of a more universal and versatile strategy continues to provide an attractive alternative, so-called modular strategy, which permits facile preparation of biosensors with tailored characteristics by a simple combination of a receptor and a signal transducer. This review describes an overview of the progress in design strategies of fluorescent biosensors, such as auto-fluorescent protein-based biosensors, protein-based biosensors covalently modified with synthetic fluorophores, and signaling aptamers, and highlights the insight into how a given receptor is converted to a fluorescent biosensor. Furthermore, we will demonstrate a significance of the modular strategy for the sensor design

    Computational Treatment of Metalloproteins

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    Metalloproteins present a considerable challenge for modeling, especially when the starting point is far from thermodynamic equilibrium. Examples include formidable problems such as metalloprotein folding and structure prediction upon metal addition, removal, or even just replacement; metalloenzyme design, where stabilization of a transition state of the catalyzed reaction in the specific binding pocket around the metal needs to be achieved; docking to metal-containing sites and design of metalloenzyme inhibitors. Even more conservative computations, such as elucidations of the mechanisms and energetics of the reaction catalyzed by natural metalloenzymes, are often nontrivial. The reason is the vast span of time and length scales over which these proteins operate, and thus the resultant difficulties in estimating their energies and free energies. It is required to perform extensive sampling, properly treat the electronic structure of the bound metal or metals, and seamlessly merge the required techniques to assess energies and entropies, or their changes, for the entire system. Additionally, the machinery needs to be computationally affordable. Although a great advancement has been made over the years, including some of the seminal works resulting in the 2013 Nobel Prize in chemistry, many aforementioned exciting applications remain far from reach. We review the methodology on the forefront of the field, including several promising methods developed in our lab that bring us closer to the desired modern goals. We further highlight their performance by a few examples of applications

    Single-molecule spectroscopy of fluorescent proteins

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