Ten Years of EU Membership – The Maltese Parliament. Occasional Paper 1/2014

Introduction. The European Union has long seen the use of enlargement as a means to transform its neighbours. For many of the 2004 enlargement countries, membership was a means to open economically and politically. For Malta and Cyprus, established democracies with extensive trade links across Europe, EU membership still had the capacity to transform their political and economic systems and hence the need, a decade on, to take stock. With this in mind and conscious that the EU political system has often raised concerns over legitimacy and accountability, attention is increasingly being focused on how the complexities of the EU political system, and the role national governments play in that system, impacts the legitimacy and accountability of the domestic political system, in particular the functioning of the national parliament. To this end, this paper will analyse how the Maltese Parliament has been impacted by membership and seek to establish whether there has been a significant alteration in its ability to hold the national executive to account.

Analysis of H.R. 12889 : a bill to amend an act entitled "An act to establish a uniform system of bankruptcy throughout the United States" approved July 1, 1898, and acts amendatory thereof and supplementary thereto and to repeal section 76 thereof and all acts and parts of acts inconsistent therewith /

"Containing amendments proposed by the National Bankruptcy Conference."

Report of the tuberculosis survey of the State Board of Health : for the twelve months from October 1, 1915, to October 1, 1916, under the provisions of Act 238 of the Public Acts of 1915 /

At head of title: State of Michigan.

Unclassified bibliographies of interest to the atomic energy program : Supplement 1 /

Cover title.

Bibliographies of interest to the atomic energy program : [Revision 1, Supplement 1] /

"November, 1959."

Biennial report of the Secretary of State of the state of Louisiana for the two years ending May 1, ... to his excellency ..., Governor of Louisiana.

Description based on: May 1, 1882.

An Analysis of Contributors to the FIU Hospitality Review: Volume 1 to Volume 19

This article documents all major articles in the FIU Hospitality Review, from its inaugural issue in spring of 1983 through 2001; 346 articles and 325 authors from 127 affiliations are included, as well as the academic institutions, hospitality industry organizations and authors who have contributed most frequently. The high ranking received by the FIU Hospitality Review is evidence of the many researchers and industry executives who have contributed over the past two decades.

Synthesis Of Linoleate Analogs With Longer Alkyl Termini To Test For Proposed "Tail-First" Binding In SBLO-1

Lipoxygenases are nonheme-iron proteins that catalyze the oxygenation of polyunsaturated fatty acids to give conjugated diene hydroperoxides. For example, soybean lipoxygenase-1 (SBLO-1) converts linoleate into 13-(S)-hydroperoxy-9(Z),11(E)-octadecadienoate (13(S)-HPOD). Although the crystal structure of SBLO-1 has been determined, it is still unclear how the substrate binds at the active site. This absence of knowledge makes it difficult to understand the role of the enzyme during catalysis of the reaction. We hypothesize that SBLO-1 binds linoleate ¿tail-first¿, so that the methyl terminus is within a hydrophobic pocket deep within the enzyme. It is believed that the hydrophobic residue phenylalanine-557 at this site has stabilizing interactions with the terminal methyl group on linoleate. To test this hypothesis, we have developed a synthetic pathway that will yield linoleate analogs with longer fatty acid chains by 1 and 2 more carbons at the alkyl terminus. These substrates will be analyzed through kinetic assays done in combination with wild type SBLO-1 and mutants in which we have replaced phenylalanine-557 with valine.

Structural studies of cytochrome P4501A1: Identification of substrate and cumene hydroperoxide binding regions in the active site of P4501A1 and characterization of the P4501A1 interaction with cytochrome P450 reductase

Cytochromes P450 are a superfamily of heme-thiolate proteins that function in a concert with another protein, cytochrome P450 reductase, as terminal oxidases of an enzymatic system catalyzing the metabolism of a variety of foreign compounds and endogenous substrates. In order to better understand P450s catalytic mechanism and substrate specificity, information about the structure of the active site is necessary. Given the lack of a crystal structure of mammalian P450, other methods have been used to elucidate the substrate recognition and binding site structure in the active center. In this project I utilized the photoaffinity labeling technique and site-directed mutagenesis approach to gain further structural insight into the active site of mammalian cytochrome P4501AI and examine the role of surface residues in the interaction of P4501A1 with the reductase. ^ Four crosslinked peptides were identified by photoaffinity labeling using diazido benzphetamine as a substrate analog. Alignment of the primary structure of cytochrome P4501A1 with that of bacterial cytochrome P450102 (the crystal structure of which is known) revealed that two of the isolated crosslinked peptides can be placed in the vicinity of heme (in the L helix region and β10-β11 sheet region of cytochrome P450102) and could be involved in substrate binding. The other two peptides were located on the surface of the protein with the label bound specifically to Lys residues that were proposed to be involved in reductase-P450 interaction. ^ Alternatively, it has been shown that some of the organic hydroperoxides can support P450 catalyzed reactions in the absence of NADPH, O2 and reductase. By means of photoaffinity labeling the cumene hydroperoxide binding region was identified. Using azidocumene as the photoaffinity label, the tripeptide T501-L502-K503 was shown to be the site where azidocumene covalently binds to P4501A1. The sequence alignment of cytochrome P4501A1 with cytochrome P450102 predicts that this region might correspond to β-sheet structure localized on the distal side of the heme ring near the I helix and the oxygen binding pocket. The role of Thr501 in the cumene hydroperoxide binding was confirmed by mutations of this residue and kinetic analysis of the effects of the mutations. ^ In addition, the role of two lysine residues, Lys271 and Lys279, in the interaction with reductase was examined by means of site-directed mutagenesis. The lysine residues were substituted with isoleucine and enzymatic activity of the wild type and the mutants were compared in reductase- and cumene hydroperoxide-supported systems. The lysine 279 residue has been shown to play a critical role in the P4501A1-reductase interaction. ^