Efficiency Analytics of NCAA Division I College Football Programs

College athletics are a multi-billion dollar industry in the United States, but how well do university athletic programs employ their resources? The question is germane in light of increasing costs of higher education and scrutiny of university budgets. This study furnishes a template to weigh the tradeoffs inherent in collegiate sports, which is the main contribution of the paper. A dataset of 117 American college football programs from 2011-2015 is analyzed using DEA and AHP methods to assess the efficiency and perception of these programs. The result is the aforementioned framework measuring the programs\u27 success and answers the question of program efficiency

Understanding the binding induced folding of intrinsically disordered proteins by protein engineering: Caveats and pitfalls

Many proteins lack a well-defined three-dimensional structure in isolation. These proteins, typically denoted as intrinsically disordered proteins (IDPs), may display a characteristic disorder-to-order transition when binding their physiological partner(s). From an experimental perspective, it is of great importance to establish the general grounds to understand how such folding processes may be explored. Here we discuss the caveats and the pitfalls arising when applying to IDPs one of the key techniques to characterize the folding of globular proteins, the Φ value analysis. This method is based on measurements of the free energy changes of transition and native states upon conservative, non-disrupting, mutations. On the basis of available data, we reinforce the validity of Φ value analysis in the study of IDPs and suggest future experiments to further validate this powerful experimental method

Estudio comparativo del sellado total de tres selladores

Buscando el éxito de la terapia endodóntica sabemos que uno de los ítems más difíciles dentro de nuestra especialidad es lograr la hermeticidad del conducto; a través de un sellador ideal. Hoy día seguimos buscando un sellador que cumpla con todos los requisitos esperados Objetivo: El objetivo de este trabajo fue estudiar en forma comparativa el sellado en la totalidad del conducto por medio de la técnica de transparentación. Los selladores endodónticos utilizados en esta oportunidad son el cemento de Grossman, el sellador de CPM Sealer y Roeko Seal.Facultad de Odontologí

Demonstration of binding induced structural plasticity in a SH2 domain

SH2 domains are common protein interaction domains able to recognize short aminoacidic sequences presenting a phosphorylated tyrosine (pY). In spite of their fundamental importance for cell physiology there is a lack of information about the mechanism by which these domains recognize and bind their natural ligands. The N-terminal SH2 (N-SH2) domain of PI3K mediates the interaction with different scaffolding proteins and is known to recognize a specific pY-X-X-M consensus sequence. These interactions are at the cross roads of different molecular pathways and play a key role for cell development and division. By combining mutagenesis, chemical kinetics and NMR, here we provide a complete characterization of the interaction between N-SH2 and a peptide mimicking the scaffolding protein Gab2. Our results highlight that N-SH2 is characterized by a remarkable structural plasticity, with the binding reaction being mediated by a diffused structural region and not solely by the residues located in the binding pocket. Furthermore, the analysis of kinetic data allow us to pinpoint an allosteric network involving residues far from the binding pocket involved in specificity. Results are discussed on the light of previous works on the binding properties of SH2 domains

The Folding Mechanism of the SH3 Domain from Grb2

SH3 domains are small protein modules involved in the regulation of important cellular pathways. These domains mediate protein-protein interactions recognizing motifs rich in proline on the target protein. The SH3 domain from Grb2 (Grb2-SH3) presents the typical structure of an SH3 domain composed of two-three stranded antiparallel \u3b2-sheets orthogonally packed onto each other, to form a single hydrophobic core. Grb2 interacts, via SH3 domain, with Gab2, a scaffolding disordered protein, triggering some key metabolic pathways involved in cell death and differentiation. In this work we report a mutational analysis (\u3c6-value analysis) of the folding pathway of Grb2-SH3 that, coupled with molecular dynamic simulations, allows us to assess the structure of the transition state and the mechanism of folding of this domain. Data suggest that Grb2-SH3 folds via a native-like, diffused transition state with a concurrent formation of native-like secondary and tertiary structure (nucleation-condensation mechanism) and without the accumulation of folding intermediates. The comparison between our data and previous folding studies on SH3 domains belonging to other proteins, highlights that proteins of this class may fold via alternative pathways, stabilized by different nuclei leading or not to accumulation of folding intermediates. This comparative analysis suggests that the alternative folding pathways for this class of SH3 domains can be selectively regulated by the specific aminoacid sequences

Estudio comparativo del sellado total de tres selladores

Buscando el éxito de la terapia endodóntica sabemos que uno de los ítems más difíciles dentro de nuestra especialidad es lograr la hermeticidad del conducto; a través de un sellador ideal. Hoy día seguimos buscando un sellador que cumpla con todos los requisitos esperados Objetivo: El objetivo de este trabajo fue estudiar en forma comparativa el sellado en la totalidad del conducto por medio de la técnica de transparentación. Los selladores endodónticos utilizados en esta oportunidad son el cemento de Grossman, el sellador de CPM Sealer y Roeko Seal.Facultad de Odontologí

Estudio comparativo del sellado total de tres selladores

Buscando el éxito de la terapia endodóntica sabemos que uno de los ítems más difíciles dentro de nuestra especialidad es lograr la hermeticidad del conducto; a través de un sellador ideal. Hoy día seguimos buscando un sellador que cumpla con todos los requisitos esperados Objetivo: El objetivo de este trabajo fue estudiar en forma comparativa el sellado en la totalidad del conducto por medio de la técnica de transparentación. Los selladores endodónticos utilizados en esta oportunidad son el cemento de Grossman, el sellador de CPM Sealer y Roeko Seal.Facultad de Odontologí

Templated folding of intrinsically disordered proteins

Much of our current knowledge of biological chemistry is founded in the structure-function relationship, whereby sequence determines structure that determines function. Thus, the discovery that a large fraction of the proteome is intrinsically disordered, while being functional, has revolutionized our understanding of proteins and raised new and interesting questions. Many intrinsically disordered proteins (IDPs) have been determined to undergo a disorder-to-order transition when recognizing their physiological partners, suggesting that their mechanisms of folding are intrinsically different from those observed in globular proteins. However, IDPs also follow some of the classic paradigms established for globular proteins, pointing to important similarities in their behavior. In this review, we compare and contrast the folding mechanisms of globular proteins with the emerging features of binding-induced folding of intrinsically disordered proteins. Specifically, whereas disorder-to-order transitions of intrinsically disordered proteins appear to follow rules of globular protein folding, such as the cooperative nature of the reaction, their folding pathways are remarkably more malleable, due to the heterogeneous nature of their folding nuclei, as probed by analysis of linear free-energy relationship plots. These insights have led to a new model for the disorder-to-order transition in IDPs termed “templated folding,” whereby the binding partner dictates distinct structural transitions en route to product, while ensuring a cooperative folding

Hidden kinetic traps in multidomain folding highlight the presence of a misfolded but functionally competent intermediate

Although more than 75% of the proteome is composed of multidomain proteins, current knowledge of protein folding is based primarily on studies of isolated domains. In this work, we describe the folding mechanism of a multidomain tandem construct comprising two distinct covalently bound PDZ domains belonging to a protein called Whirlin, a scaffolding protein of the hearing apparatus. In particular, via a synergy between NMR and kinetic experiments, we demonstrate the presence of a misfolded intermediate that competes with productive folding. In agreement with the view that tandem domain swapping is a potential source of transient misfolding, we demonstrate that such a kinetic trap retains native-like functional activity, as shown by the preserved ability to bind its physiological ligand. Thus, despite the general knowledge that protein misfolding is intimately associated with dysfunction and diseases, we provide a direct example of a functionally competent misfolded state. Remarkably, a bioinformatics analysis of the amino acidic sequence of Whirlin from different species suggests that the tendency to perform tandem domain swapping between PDZ1 and PDZ2 is highly conserved, as demonstrated by their unexpectedly high sequence identity. On the basis of these observations, we discuss on a possible physiological role of such misfolded intermediate