972 research outputs found
La recente riforma dei reati contro la pubblica amministrazione
No full textaddenda a FIANDACA - MUSCO, Diritto penale. Parte speciale,
Per lo studio delle religioni: un nuovo strumento di lavoro.
No full textPresentazione del volume di Giulia SFAMEMI GASPARRO, Introduzione alla storia della religione, Editori Laterza, Roma-Bari 2011. Interventi di MASSIMO NARO e NICOLA CUSUMANO. Presentazione di ALESSANDRO MUSCO
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No full textStudio del film "Lo smemorato" di Gennaro Righelli con Angelo Musco alla luce dei rapporti con il fascismo, "Il fu Mattia Pascal" di Luigi Pirandello e il caso giudiziario Bruneri-Canella
Reaction of trans-{PtH2[P(C6H11)3]2} with carbon disulphide. Kinetic study of the insertion reaction and X-ray structure of trans-{PtH(S2CH)[P(C6H11)3]2}
No full textCarbon disulphide inserts into the PtH bond of trans-{PtH2[P(C6H11)3]2} to give trans-{PtH(S2CH) [P(C6H11)3]2}. The X-ray structure shows that the -S2CH group is bonded to the metal through a sulfur atom as a monodentate thioformate anion. The kinetics of the carbon disulfide insertion have been investigated. The results account for a mechanism involving CS2 addition to trans-{PtH2[P(C6H113]2} to give a five-coordinate intermediate, which collapses to trans-{PtH(S2CH)[P(C6H11)3]2}
HMGB1-Carbenoxolone Interactions: Dynamics Insights from Combined Nuclear Magnetic Resonance and Molecular Dynamics
No full textThe interplay of protein dynamics and molecular recognition is of
fundamental importance in biological processes. Atomic-resolution
insights into these phenomena may provide new opportunities for drug
discovery. Herein, we have combined NMR relaxation experiments and
residual dipolar coupling (RDC) measurements with molecular dynamics
(MD) simulations to study the effects of the anti-inflammatory drug
carbenoxolone (CBNX) on the conformational properties and on the
internal dynamics of a subdomain (box A) of high-mobility group B
protein (HMGB1). (15)N relaxation data show that CBNX binding enhances
the fast pico- to nanosecond motions of a loop and partially removes the
internal motional anisotropy of the first two helices of box A. Dipolar
wave analysis of amide RDC data shows that ligand binding induces
helical distortions. In parallel, increased mobility of the loop upon
ligand binding is highlighted by the essential dynamics analysis (EDA)
of MD simulations. Moreover, simulations detect two possible
orientations for CBNX, which induces two possible conformations of helix
H3, one being similar to the free form and the second one causing a
partial helical distortion. Finally, we introduce a new approach for the
analysis of the internal coordination of protein residues that is
consistent with experimental data and allows us to pinpoint which
substructures of box A are dynamically affected by CBNX. The
observations reported here may be useful for understanding the role of
protein dynamics in binding at atomic resolution
Faunal and biogeographic analysis of Syllidae (Polychaeta) from Rovinj (Croatia, northern Adriatic Sea)
No full textThe study of hard-bottom Syllidae (Polychaeta) of the Rovinj area provides an updated measure of syllid species diversity in the northern Adriatic Sea. Faunal research in the coldest Mediterranean sectors may also help to address possible ecological and biogeographical consequences arising from climate change. Thirty-nine species were found, of which 13 are new for the northern Adriatic, increasing the species recorded from the area from 53 to 66. Some newly recorded species are dominant and typical of warmer areas. The lack of previous taxonomic updates is responsible for the high number of new findings. However, the northern Adriatic Sea is possibly undergoing long-term changes, with modifications of diversity due to the establishment of warm-water species. Syllid fauna of Sveti Ivan Island and its bioclimatic affinity are, in fact, unexpectedly more similar to the ones of some southern Mediterranean areas than to those traditionally reported for the northern Adriatic
Interactions of the C2 domain of human factor V with a model membrane
No full textActivated coagulation Factor V is an important cofactor of the coagulation cascade that catalyzes the formation, of the prothrombinase complex on. the surface of membranes rich in phosphatidyl-L-serine (PS). Here we report molecular dynamics simulations of the two crystallographic structures (the open and closed conformations) of domain C2 of coagulation Factor V (FaVC2). The calculations were performed in water (1.5 ns for each conformation) and in the presence of a neutral phospholipid bilayer model (POPE; 10 ns for each conformation) in order to describe the dynamics of the free (plasma circulating) and membrane bound forms of FaVC2. Water simulations confirmed the hypothesis that the plasma circulating form is in the closed conformation. In contrast, the membrane simulations showed that both conformations are energetically compatible with membrane binding. We have investigated the mechanism, the dynamics, and the energetics of the binding process. Our data are consistent with published estimates of the immersion depth of the aromatic residues (W26 and W27), and with mutagenesis studies involving specific residues located on the spikes at the bottom of the FaVC2 structure. Electrostatic interactions between the phospholipid head groups and hydrophilic residues at the bottom of the structure play a key role in the binding process by creating a large number of hydrogen bonds that anchor the protein to the membrane. The simulations identified a stable phospholipid binding pocket reminiscent of a previously suggested PS interaction site. Our structural data could contribute to the design of potential inhibitors able to disrupt membrane association
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