Visualization of Simulations of a Robot Operated Car Park System

Magistritöö „Robotiseeritud parkimissüsteemi simulatsioonide visualiseerimine“ eesmärgiks on identifitseerida parimad praktikad ja tehnoloogiad robotiseeritud parkimissüsteemi algoritmi efektiivsuse esitlemiseks potentsiaalsetele klientidele. Magistritöös leitud praktikaid ja tehnoloogiaid kasutades luuakse robotite tööd demonstreeriv veebirakendus. Töö lõpus hinnatakse rakenduse pakutavat kasutajakogemust ning vastavust seatud nõuetele.The aim of the MA thesis "Visualization of simulations of a robot operated car park system" is to identify the best practices and technologies to present the effectiveness of robot operated car park system's underlying algorithm to potential customers. An application demonstrating the work of the robots is built using the identified technologies and best practices. The user experience of the application and the application's compliance to the requirements of the tool are validated in the thesis

Data Integration from Different Web Sites in a Used Car Web Portal

Kasutatud auto ostmine võib olla pikk ja riskantne protsess. Käesolevas töös maandatakse kasutatud auto ostmisega kaasnevaid riske parandades ostja informeeritust koondades auto andmed ühte kohta. Valminud veebiportaal annab kasutajale kuulutuse andmete põhjal ülevaate auto ajaloost ja tehnilistest andmetest. Valminud portaal kasutab erinevaid veebi-põhiseid liidestamise võtteid erinevatest veebiallikatest vajaliku info kogumiseks.Buying a used car can be a long and risky process. In this paper the risks of buying a used car are lowered by bringing data of the car together in a used car portal, which will im-prove buyer’s awareness. The web portal gives a review of the history and technical data of the car. Several different integration techniques were used in the development of the web portal

Proteolytic profile of Treponema vincentii ATCC 35580 with special reference to collagenolytic and arginine aminopeptidase activity

Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/73401/1/j.1399-302X.1988.tb00096.x.pd

Increased consumption of fruit and vegetables for the primary prevention of cardiovascular diseases

There is increasing evidence that high consumption of fruit and vegetables is beneficial for cardiovascular disease (CVD) prevention

Identification and Characterization of Prokaryotic Dipeptidyl-Peptidase 5 from Porphyromonas gingivalis

Porphyromonas gingivalis, a Gram-negative asaccharolytic anaerobe, is one of the major causative organisms of chronic periodontitis. The bacterium utilizes amino acids as energy and carbon sources, and incorporates them mainly as dipeptides. Therefore, a wide variety of dipeptide production processes mediated by dipeptidyl-peptidases (DPPs) should be beneficial for the organism. In the present study, we identified the fourth P. gingivalis enzyme, DPP5. A DPP7-like activity still remained in a dpp4-7-11 disrupted P. gingivalis ATCC 33277. PGN_0756, currently annotated as a prolyl oligopeptidase, possessed an activity indistinguishable from that of the triple dpp gene-disrupted strain, and was identified as a bacterial orthologue of fungal DPP5, because of its substrate specificity and 28.5% amino acid sequence identity with an Aspergillus fumigatus entity. P. gingivalis DPP5 was composed of 684 amino acids with an apparent molecular weight of 66 kDa, while it preferred Ala and hydrophobic residues, had no activity toward Pro at the P1 position, and no preference for hydrophobic P2 residues, showed an optimal pH of 6.7 in the presence of NaCl, demonstrated kcat/Km values for Gly-Phe-MCA and Lys-Ala-MCA of 13.01 and 11.02 μM-1 s-1, respectively, and was localized in the periplasm. DPP5 elaborately complemented DPP7 in liberation of dipeptides with hydrophobic P1 residues. Examinations of dpp- and gingipain gene-disrupted mutants indicated that DPP4, DPP5, DPP7, and DPP11 together with Arg- and Lys-gingipains cooperatively liberate most dipeptides from nutrient oligopeptides. This is the first study to report that DPP5 is expressed not only in eukaryotes, but also distributed in prokaryotes

Identification of Dipeptidyl-Peptidase (DPP)5 and DPP7 in Porphyromonas endodontalis, Distinct from Those in Porphyromonas gingivalis

Dipeptidyl peptidases (DPPs) that liberate dipeptides from the N-terminal end of oligopeptides are crucial for the growth of Porphyromonas species, anaerobic asaccharolytic gram negative rods that utilize amino acids as energy sources. Porphyromonas endodontalis is a causative agent of periapical lesions with acute symptoms and Asp/Glu-specific DPP11 has been solely characterized in this organism. In this study, we identified and characterized two P. endodontalis DPPs, DPP5 and DPP7. Cell-associated DPP activity toward Lys-Ala-4-methylcoumaryl-7- amide (MCA) was prominent in P. endodontalis ATCC 35406 as compared with the Porphyromonas gingivalis strains ATCC 33277, 16-1, HW24D1, ATCC 49417, W83, W50, and HNA99. The level of hydrolysis of Leu-Asp-MCA by DPP11, Gly- Pro-MCA by DPP4, and Met-Leu-MCA was also higher than in the P. gingivalis strains. MER236725 and MER278904 are P. endodontalis proteins belong to the S9- and S46-family peptidases, respectively. Recombinant MER236725 exhibited enzymatic properties including substrate specificity, and salt- and pH-dependence similar to P. gingivalis DPP5 belonging to the S9 family. However, the kcat/Km figure (194 mM21?sec21) for the most potent substrate (Lys-Ala-MCA) was 18.4-fold higher as compared to the P. gingivalis entity (10.5 mM21?sec21). In addition, P. endodontalis DPP5 mRNA and protein contents were increased several fold as compared with those in P. gingivalis. Recombinant MER278904 preferentially hydrolyzed Met-Leu-MCA and exhibited a substrate specificity similar to P. gingivalis DPP7 belonging to the S46 family. In accord with the deduced molecular mass of 818 amino acids, a 105-kDa band was immunologically detected, indicating that P. endodontalis DPP7 is an exceptionally large molecule in the DPP7/DPP11/S46 peptidase family. The enhancement of four DPP activities was conclusively demonstrated in P. endodontalis, and remarkable Lys-Ala-MCAhydrolysis was achieved by qualitative and quantitative potentiation of the DPP5 molecule