892 resultados para sheet metal design
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This layer is a georeferenced raster image of the Soviet Army topographic sheet map covering a portion of the Zhejiang Sheng region, China (map quadrangle number: H-50-XXIV). It is from a series of Soviet Army topographic maps of China 1:200,000. The source map was published in 1979. The image inside the map neatline is georeferenced to the surface of the earth and fit to the Pulkovo 1942 GK Zone 20N projection. Map collar information from the source map have been cropped and are not available as part of the raster image. China 1:200,000 topographic maps were prepared and printed by the Soviet Army General Headquarters, 1976-1991. China 1:200,000 maps are in Russian. Each source map in the series is printed in color. China 1:200,000 maps are typical topographic maps portraying both natural and manmade features. They show and name works of nature, such as mountains, valleys, lakes, rivers, vegetation, etc. They also identify the principal works and structures of humans, such as roads, railroads, paths, walls, boundaries, transmission lines, major buildings, etc. Relief is shown with standard contour intervals of 40 meters and/or spot heights.
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This layer is a georeferenced raster image of the Soviet Army topographic sheet map covering a portion of the Zhejiang Sheng region, China (map quadrangle number: H-50-XXX). It is from a series of Soviet Army topographic maps of China 1:200,000. Published in 1979, the source map was compiled from maps 1:100,000 published in 1977; corrected according to source material, 1970-1975. The image inside the map neatline is georeferenced to the surface of the earth and fit to the Pulkovo 1942 GK Zone 20N projection. Map collar information from the source map have been cropped and are not available as part of the raster image. China 1:200,000 topographic maps were prepared and printed by the Soviet Army General Headquarters, 1976-1991. China 1:200,000 maps are in Russian. Each source map in the series is printed in color. China 1:200,000 maps are typical topographic maps portraying both natural and manmade features. They show and name works of nature, such as mountains, valleys, lakes, rivers, vegetation, etc. They also identify the principal works and structures of humans, such as roads, railroads, paths, walls, boundaries, transmission lines, major buildings, etc. Relief is shown with standard contour intervals of 40 meters and/or spot heights.
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National Highway Traffic Safety Administration, Office of Research and Development, Washington, D.C.
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"August 31, 1962."
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"UILU-ENG 79 1745"--Cover.
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"July 15, 1971."
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"Contract AT(30-1)-2789."
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"Contract AT(30-1)-2789."
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"Contract AT(30-1)-2789."
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Mode of access: Internet.
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Photocopy.
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Errata sheet at end.
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Inserted "Bibliographic data sheet" lists Gerald H. Adams as editor.
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Alpha helices are key structural components of proteins and important recognition motifs in biology. New techniques for stabilizing short peptide helices could be valuable for studying protein folding, modeling proteins, creating artificial proteins, and may aid the design of inhibitors or mimics of protein function. We previously reported* that 5-15 residue peptides, corresponding to the Zn-binding domain of thermolysin, react with [Pd(en)(ONO,),]in DMF-d’ and 90% H,O 10% DzO to form a 22-membered [Pd(en)(H*ELTH*)]2+ macrocycle that is helical in solution and acts as a template in nucleating helicity in both Cand N- terminal directions within the longer sequences in DMF. ~f~~&g7$$& d&qx~m ~. y AC&q& In water, however, there was less a-helicity observed, testifying to #..q,& &$--Lb &l-- &.$;,J~p?:~~q&~+~~ ’ w w the difficulty of fixing intramolecular amide NH...OC H-bonds in 6,“;;” ( k.$ U”C.a , p d$. competition with the H-bond donor solvent water. To expand the utility of [Pd(en)(H*XXXH*)]*+ as a helix- @r4”8 & oJ#:& &G& @-qd ,‘d@-gyp promoting module in solution, we now report the result that Ac- ‘$4: %$yyy + H*ELTH*H*VTDH*-NH,(l), AC-H*ELTH*AVTDYH*ELTH*- NH, (2) and AC-H*AAAH*H*ELTH*H*VTDH*-NH* (3) react with multiple equivalents of [Pd(en)(ONO,),] to produce exclusively 4-6 respectively in both DMF-d7 and water (90% Hz0 10% D,O). Mass spectrometry, 15N- and 2D ‘H- NMR spectroscopy, and CD spectra were used to characterise the structures 4-6, and their three dimensional structures were calculated from NOE restraints using simulated annealing protocols. Results demonstrate (a) selective coordination of metal ions at (i, i+4) histidine positions in water and DMF, (b) incorporation of 2 and 3 a turn-mimicking modules [Pd(en)(HELTH)]2+ in lo-15 residue peptides, and (c) facile conversion of unstructured peptides into 3- and 4- turn helices of macrocycles, with well defined a-helicity throughout and more structure in DMF than in water.
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Biological utilisation of copper requires that the metal, in its ionic forms, be meticulously transported, inserted into enzymes and regulatory proteins, and excess be excreted. To understand the trafficking process, it is crucial that the structures of the proteins involved in the varied processes be resolved. To investigate copper binding to a family of structurally related copper-binding proteins, we have characterised the second Menkes N-terminal domain (MNKr2). The structure, determined using H-1 and N-15 heteronuclear NMR, of the reduced form of MNKr2 has revealed two alpha-helices lying over a single beta-sheet and shows that the binding site, a Cys(X)(2)Cys pair, is located on an exposed loop. H-1-N-15 HSQC experiments demonstrate that binding of Cu(I) causes changes that are localised to conserved residues adjacent to the metal binding site. Residues in this area are important to the delivery of copper by the structurally related Cu(I) chaperones. Complementary site-directed mutagenesis of the adjacent residues has been used to probe the structural roles of conserved residues. (C) 2003 Published by Elsevier Inc.