�ݺ�ߣshows by User: ant0n1us

�ݺ�ߣshows by User: ant0n1us / http://www.slideshare.net/images/logo.gif �ݺ�ߣshows by User: ant0n1us / Fri, 20 Nov 2009 13:16:24 GMT �ݺ�ߣShare feed for �ݺ�ߣshows by User: ant0n1us Cool Ahsg Model /ant0n1us/cool-ahsg-model-2548169 coolahsgmodel-1258744523064-phpapp02
Fig. 14. A cartoon representation of the two structural faces of secreted Ahsg. There is no X-ray crystallographic or NMR-derived structure on which to base the 3-dimensional folding of Ahsg from any species. However, bioinformatics tools can be used to simulate a model which suggests recognition of hydroxyapatite by the C-terminal cystatin homology domains (residues 18-248; dotted red ovals), and the Fn3 homology domains of the insulin receptor by Ahsg residues 249-367 (dotted blue oval). The 350-residue single chain of human Ahsg (residues 18-367) was submitted to the I-TASSER website (Zhang, 2008), which uses amino acid homology of submitted protein sequences with protein sequences in the PDB database, and returns five models. I stipulated that I-TASSER take into consideration the known 5 disulfide pairs in Ahsg using the “Assign contact/distance restraints” feature, and chose Model 5 from Run S34302. PyMol for Mac (http://www.pymol.org/) to visualize the resulting pdb-formatted file generated by I-TASSER. Some of the –S-S- bonds are depicted in orange. Regions of strong α-helicity are colored blue; β-sheet structures yellow, and the unstructured backbone colored green.]]>
Fig. 14. A cartoon representation of the two structural faces of secreted Ahsg. There is no X-ray crystallographic or NMR-derived structure on which to base the 3-dimensional folding of Ahsg from any species. However, bioinformatics tools can be used to simulate a model which suggests recognition of hydroxyapatite by the C-terminal cystatin homology domains (residues 18-248; dotted red ovals), and the Fn3 homology domains of the insulin receptor by Ahsg residues 249-367 (dotted blue oval). The 350-residue single chain of human Ahsg (residues 18-367) was submitted to the I-TASSER website (Zhang, 2008), which uses amino acid homology of submitted protein sequences with protein sequences in the PDB database, and returns five models. I stipulated that I-TASSER take into consideration the known 5 disulfide pairs in Ahsg using the “Assign contact/distance restraints” feature, and chose Model 5 from Run S34302. PyMol for Mac (http://www.pymol.org/) to visualize the resulting pdb-formatted file generated by I-TASSER. Some of the –S-S- bonds are depicted in orange. Regions of strong α-helicity are colored blue; β-sheet structures yellow, and the unstructured backbone colored green.]]> Fri, 20 Nov 2009 13:16:24 GMT /ant0n1us/cool-ahsg-model-2548169 ant0n1us@slideshare.net(ant0n1us) Cool Ahsg Model ant0n1us Fig. 14. A cartoon representation of the two structural faces of secreted Ahsg. There is no X-ray crystallographic or NMR-derived structure on which to base the 3-dimensional folding of Ahsg from any species. However, bioinformatics tools can be used to simulate a model which suggests recognition of hydroxyapatite by the C-terminal cystatin homology domains (residues 18-248; dotted red ovals), and the Fn3 homology domains of the insulin receptor by Ahsg residues 249-367 (dotted blue oval). The 350-residue single chain of human Ahsg (residues 18-367) was submitted to the I-TASSER website (Zhang, 2008), which uses amino acid homology of submitted protein sequences with protein sequences in the PDB database, and returns five models. I stipulated that I-TASSER take into consideration the known 5 disulfide pairs in Ahsg using the “Assign contact/distance restraints” feature, and chose Model 5 from Run S34302. PyMol for Mac (http://www.pymol.org/) to visualize the resulting pdb-formatted file generated by I-TASSER. Some of the –S-S- bonds are depicted in orange. Regions of strong α-helicity are colored blue; β-sheet structures yellow, and the unstructured backbone colored green. <img style="border:1px solid #C3E6D8;float:right;" alt="" src="https://cdn.slidesharecdn.com/ss_thumbnails/coolahsgmodel-1258744523064-phpapp02-thumbnail.jpg?width=120&height=120&fit=bounds" /><br> Fig. 14. A cartoon representation of the two structural faces of secreted Ahsg. There is no X-ray crystallographic or NMR-derived structure on which to base the 3-dimensional folding of Ahsg from any species. However, bioinformatics tools can be used to simulate a model which suggests recognition of hydroxyapatite by the C-terminal cystatin homology domains (residues 18-248; dotted red ovals), and the Fn3 homology domains of the insulin receptor by Ahsg residues 249-367 (dotted blue oval). The 350-residue single chain of human Ahsg (residues 18-367) was submitted to the I-TASSER website (Zhang, 2008), which uses amino acid homology of submitted protein sequences with protein sequences in the PDB database, and returns five models. I stipulated that I-TASSER take into consideration the known 5 disulfide pairs in Ahsg using the “Assign contact/distance restraints” feature, and chose Model 5 from Run S34302. PyMol for Mac (http://www.pymol.org/) to visualize the resulting pdb-formatted file generated by I-TASSER. Some of the –S-S- bonds are depicted in orange. Regions of strong α-helicity are colored blue; β-sheet structures yellow, and the unstructured backbone colored green.

Cool Ahsg Model from ant0n1us

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