679 research outputs found
Refrigerator
No full textThe ornamental design of a refrigerator as shown and described.
[0001] 1. Refrigerator
[0002] 1.1 Front perspective view with the door in the open position;
[0003] 1.2 Front perspective view with the door in the close position;
[0004] 1.3 Front view with the door in the open position;
[0005] 1.4 Rear view with the door in the open position; and
[0006] 1.5 : Right side view
[0007] 1.6 : Left side view
[0008] 1.7 Top view with the door in the open position
Computational and biochemical studies of the TagA enzyme inform cellular localization.
No full text(A) A model of full-length TagA was constructed with experimentally determined TagAΔC (surface representation) and the C-terminal domain, which was modeled by GREMLIN structural prediction (cartoon representation). Three C-terminal helices appear to complete the active site and obstruct the dimeric interface of TagAΔC. Highly conserved (magenta), moderately conserved (white) and weakly conserved (teal) residues are indicated for the TagAΔC crystal structure. (B) Helical wheel projections of helix H11 in TagA homologs predict a putative amphipathic helix. (C) TagA associates with the bacterial cell membrane. Immunoblots of cellular fractionation indicate that B. subtilis TagA is exclusively localized to the membrane (M), while TagAΔC is primarily localized in the supernatant (S). Samples were fractionated by ultracentrifugation identically and the BsTagA-FL blot was exposed for 10 minutes, the BsTagA-V196 blot was exposed for 1 minute, and the BsTagA-ΔH11 blot was exposed for 30 seconds. (D) TagA is a peripheral membrane protein. Chaotropic and alkaline treatments of B. subtilis TagA reveal that the enzyme is peripherally associated with the membrane and is more effectively displaced by alkaline treatment. Treated membrane fractions were loaded onto a sucrose cushion, centrifuged, and carefully separated into bottom (B; pellet), middle (M; sucrose cushion volume), and top (T; sample volume).</p
Sauna taga tiigi ääres....
No full texthe folklorisation process of authorial songs is by no means a remnant of the past. The works of local song composers circulate among wider public independently from their author's will.The modern type of rhymed South-Estonian folk song of the recent years is represented in the works of poets Jaan Pulk, Jan Rahman, Contra (Margus Konnula) and many others.Two South-Estonian authorial songs Haani miis [The Haanja Man] and Sauna taga tiigi ääres [At the Pond behind the Sauna] have been sung all over Estonia since the end of the 19th and the beginning of the 20th century. Today, these two songs are known as folksongs. The first was composed by Jaan Räppo (b. on April 11th, 1880 in Võrumaa - died on April 14th, 1958), also known as a politician and cultural figure in the Ukraine. In 1897 he wrote the verse narrative about a poor man from Kasaritsa while studying at the Võru town school in Estonia.The song Sauna taga tiigi ääres was composed by Hermann Julius Schmalz (b. on April 6th, 1870 in Räpina parish on the border of Võru and Setu region). According to the poet and literate himself he had not attended school for a day in his life; instead, he was educated (among other things in German language) by his mother and governess, also by independent study. As a youth he learned to play several folk music instruments, violin, piano and guitar, he could also read music
Model of the TagA enzyme-substrate complex and mechanism of catalysis.
No full text(A) The proposed active site of TagA co-localizes residues D65, T37, and R221. Lipid-α (yellow) is activated by the catalytic base D65 (pink), while ManNAc (green) is positioned by contacts between its C6 hydroxyl and T37 (cyan). The C-terminal helices (tan) are modeled according to GREMLIN structural predictions and place R221 (purple) adjacent to the phosphates of UDP-ManNAc (orange) to putatively stabilize the leaving group. (B) The TagA molecular mechanism is proposed to utilize a dimer to monomer transition to regulate glycosyltransferase activity. TagA is stabilized as a soluble dimer. Upon interaction with the cell membrane, the C-terminus adopts an ordered state and disrupts the dimer interface, which produces a competent active site by co-localizing D65, T37, and R221 to coordinate the soluble UDP-ManNAc and membrane-bound lipid-α substrates. (C) TagA reveals the catalytic mechanism of the GT26 family. Asp65 activates lipid-α, which proceeds to attack UDP-ManNAc in an SN2-like mechanism. Coordination between Arg221 and the phosphates of UDP stabilize the leaving group, permitting the oxocarbenium ion-like transition state. The mechanism is completed by glycosidic bond-formation between GlcNAc and ManNAc to form lipid-β.</p
Cellular and molecular large-scale features of fetal adipose tissue: is bovine perirenal adipose tissue brown?
No full text<i>In silico</i> substrate binding and mechanistic studies of TagA.
No full text(A) Structure of the UDP:TagAΔC complex. A simulated annealing omit map contoured at 3σ reveals that the β-phosphate of UDP (orange) in the UDP:TagAΔC structure is adjacent to the proposed catalytic base, Asp65 (pink), and putative ManNAc stabilizing residue, Thr37 (cyan). The uracil nucleoside is pi-stacked over Tyr137. (B) Consurf analysis reveals that UDP projects its phosphates (orange) into the pocket and is coordinated by a pocket of highly conserved residues. Highly conserved (magenta), moderately conserved (white) and weakly conserved (teal) residues are indicated. (C) In silico generated model of TagAΔC bound to its substrates. The model contains a lipid-α analog (yellow) and UDP-ManNAc (green). The electrostatic surface of the protein is shown. Negatively charged residues (red), neutral residues (white), positively charged residues (blue) are shown. The coordinates of the model were generated using a two-step procedure. First, the coordinates of the ligand-bound UDP:TagAΔC crystal structure were used to restrain the positioning of UDP-ManNAc. Autodock vina was then used to dock lipid-α. The docking results positioned the non-reducing end of GlcNAc toward the C4 in ManNAc when bound to the TagAΔC dimer. (D) The upper panel indicates the reaction scheme used for the in vitro TagA activity assay. 200 nM TagA enzyme was incubated at 30°C with 100 μM lipid-α substrate analog and UDP-ManNAc produced in situ from UDP-GlcNAc by the epimerase MnaA, followed by quenching with 4M urea. Conversion of UDP-ManNAc to UDP is monitored at 271 nm using a DNAPak PA200 anion exchange column. The lower panel indicates activity measurements of T. italicus and S. aureus TagA enzymes from the in vitro TagA activity assay, as described above. Reactions with error bars were performed in triplicate, and asterisks indicate p<0.005 by Student’s T-test.</p
Sokerimäärityksissä huomioon otettavia yksityiskohtia
No full textvKirjasto Aj-kDetaljer som man bör taga hänsyn till vid sockerbestämningar Details in determination of sugar
The WTA linkage unit and TagA structural characteristics.
No full text(A) WTA linkage unit and polymer. The linkage unit is attached to the peptidoglycan via the C6-hydroxyl of N-acetylmuramic acid and is composed of a GlcNAc (TagO-catalyzed), ManNAc (TagA-catalyzed), and n = 2–3 glycerol phosphates (TagB- and TagF-catalyzed). R = glycerol or ribitol, m = 40–60. (B) Cartoon ribbon representation of TagAΔC from T. italicus. Apo-TagAΔC crystallizes as a dimer. The dimer interface is over 1000 Å in surface area and is formed by buried hydrophobic residues. (C) TagAΔC protomer with secondary structural elements indicated. H = alpha helix, β = beta strand. (D) Electrostatic surface representation of the TagAΔC dimer. Negatively charged (red), neutral (white), and positively charged (blue) residues are indicated. Rotation of 180° about the dimer interface allows visualization of the pore.</p
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