published_or_final_version / Mechanical Engineering / Master / Master of Philosophy

No description available.

The ever-increasing number of devices capable of, not only connecting to existing communication networks, but also, independently creating new ones is defining a new communication network, in which the Internet is only one of the substrate networks pro- viding connectivity between diverse devices. This is a network with many interconnected mobile devices connecting to infrastructure networks and creating their own dynamic substrate networks. We present a novel routing scheme for diverse collections of substrate networks with a mix of mobile and static nodes. A key element of the routing scheme is to utilize the exiting routing paths in substrate networks, and set up routing paths between substrate networks. We use sets of nodes as landmarks and define locators that describe node position in the network relative to landmarks. This allows our routing scheme to scale to a large number of nodes, as only information about landmarks needs to be propagated throughout the network.

The ever-increasing number of devices capable of, not only connecting to existing communication networks, but also, independently creating new ones is defining a new communication network, in which the Internet is only one of the substrate networks pro- viding connectivity between diverse devices. This is a network with many interconnected mobile devices connecting to infrastructure networks and creating their own dynamic substrate networks. We present a novel routing scheme for diverse collections of substrate networks with a mix of mobile and static nodes. A key element of the routing scheme is to utilize the exiting routing paths in substrate networks, and set up routing paths between substrate networks. We use sets of nodes as landmarks and define locators that describe node position in the network relative to landmarks. This allows our routing scheme to scale to a large number of nodes, as only information about landmarks needs to be propagated throughout the network.

YchM is the sole E. coli member of the SLC26 superfamily of anion transporters, which are characterized by an N-terminal transport domain and a C-terminal cytosolic STAS (Sulphate Transporter and Anti-Sigma factor antagonist) domain. In a previous study, the STAS domain of YchM co-purified and crystallized with acyl carrier protein (ACP). In this study, analysis of the ACP-STAS interaction using isothermal titration calorimetry (ITC) showed that the 4’phosphopantetheine of ACP and R523 and R527 of the STAS are crucial for binding. The binding constant for the ACP-STAS interaction was found to be 0.7 +/- 0.1 μM. The potential role of YchM for pH regulation and fatty acid degradation studied in vivo indicated that a) YchM does not provide selective advantage for growth in alkaline pH and b) YchM was not essential for cell growth, even when fatty acids were the sole carbon source.

YchM is the sole E. coli member of the SLC26 superfamily of anion transporters, which are characterized by an N-terminal transport domain and a C-terminal cytosolic STAS (Sulphate Transporter and Anti-Sigma factor antagonist) domain. In a previous study, the STAS domain of YchM co-purified and crystallized with acyl carrier protein (ACP). In this study, analysis of the ACP-STAS interaction using isothermal titration calorimetry (ITC) showed that the 4’phosphopantetheine of ACP and R523 and R527 of the STAS are crucial for binding. The binding constant for the ACP-STAS interaction was found to be 0.7 +/- 0.1 μM. The potential role of YchM for pH regulation and fatty acid degradation studied in vivo indicated that a) YchM does not provide selective advantage for growth in alkaline pH and b) YchM was not essential for cell growth, even when fatty acids were the sole carbon source.

The topic of the paper is the legal aspects of the use of domain names in the electronic space. The domain names are the new individualization tools that are not entered into the system yet. Due to the existing situation the conflicts of interests of the owners of the domain names on one hand and the owners of other individualization tools on the other hand arise. The solution of these disputes that are still very new and very specific causes a lot of problems to the law institutions as well as to legal bodies and natural persons. The goal of the paper is the problems, which arise to the registration and use of the domain names and other individualization tools, such as trade names, personal names, etc., analysis. The paper analyses the procedure of the composition of the domain names and the regulations of their registration. It also deals with the problems related to the registration of the domain names and their use in the electronic space. Efforts have been made to look into conflicts between the domain names and other tools of individualization. The document of „The Uniform Domain Names Dispute Resolution Policy“ adopted by the Internet Corporation for Assigned Names And Numbers and the practice of the courts abroad is being analyzed.

INDETERMINATE DOMAIN (IDD) genes encode a large family of putative transcription factors characterized by four different zinc finger motifs in a conserved arrangement. In Arabidopsis thaliana there are 16 IDD genes designated AtIDD1-AtIDD16. Microarray database expression resources show that AtIDD1 transcripts are present at high levels in dry seed and in response to abscisic acid. Transcripts present in dry seed at high levels have previously been shown to play roles in later stages of seed development or as provisions necessary for the resumption of metabolic activity following seed dormancy. Here I show that lines with constitutive expression of AtIDD1 have decreased and increased sensitivity to the phytohormones abscisic acid and gibberellic acid, respectively, when applied exogenously. Additionally, plants overexpressing AtIDD1 have altered mucilage extrusion and seed coat morphology. Altered seed coat morphology was also observed In constitutive AtIDD1 knock down lines. Therefore, these phenotypes could indicate that AtIDD1 plays a regulatory role in seeds during seed development and/or germination.

The prothrombinase (IIase) complex is an essential component of the coagulation cascade and is composed of a serine protease, Factor Xa (FXa), its non-enzymatic cofactor, Factor Va (FVa), calcium and a phospholipid membrane surface. It activates prothrombin (FII) to thrombin, the principal stimulator of clot formation in vivo. FII activation by IIase is mediated by specific interactions between FII and FVa. Preliminary NMR and peptidyl mimicry studies identified six residues within the FII Fragment 2 (F2) domain (S160, Q177, R181, L182, V184 and T185) that likely mediate an interaction between it and the heavy chain of FVa. Therefore, six recombinant FII derivatives were prepared whereby each of the aforementioned residues was mutated to alanine. FII activation kinetics by FXa in the presence or absence of FVa was measured by DAPA-thrombin complex formation. The results show that FII-S160A, -R181A, -L182A, -V184A and -T185A had no significant effect on the catalytic efficiency of the reaction in the presence of FVa. In the absence of FVa, the catalytic efficiency of FII-R181A, -L182A, -V184A, and -T185A derivatives decreased by 17-27% compared with wildtype, while FII-S160A had no effect. FII-Q177A, however, showed a significant increase of 17% in catalytic efficiency in the presence of FVa but no change in its absence. Two double (FII-Q177A/R181A and FII-R181A/T185A) and one triple (FII-Q177A/R181A/T185) mutants were generated to determine if multiple mutations would have an additive effect. These derivatives were indistinguishable from wildtype in the presence of FVa. In the absence of FVa, however, their catalytic efficiency values decreased 12-25% compared with wildtype. Further comparison of these values showed that FII-R181A and -Q177A/R181A both decreased by 25%, while FII-R181A/T185A and -Q177A/R181A/T185A decreased by 12% and 24% with respect to the wildtype, respectively. Both comparisons, where the only difference was an additional mutation at Q177, suggest that Q177 does not affect the activation kinetics of FII in the absence of FVa. Taken together, our data suggest that Q177 in the F2 domain of FII is likely involved in interacting with IIase through a FVa-dependent mechanism while residues R181, L182, V184 and T185 may be involved through a FVa-independent mechanism. / Thesis (Master, Biochemistry) -- Queen's University, 2012-07-31 11:38:32.262

No description available.