Sandbox GGC5: Difference between revisions

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•This is the <scene name='78/781193/Titin_rainbow_tc/1'>rainbow</scene> version of the titin molecule. This structure is colored to differentiate each chain, starting with the blue 5' amino end, ending with the red 3' carboxyl end.

•This secondary structure of titin highlights the <scene name='78/781193/Hydrophobic_structure_tc/1'>polar.</scene> sections of the titin molecule. In this representation, Polar sections of titin are shaded in purple and hydrophobic regions are shaded in grey. The central beta-sandwich structure of the molecule encloses a well defined hydrophobic core. This helps to stabilize the molecule that contains no disulfide bridges and rely solely on hydrogen bonding in the side chains and backbone.

•This secondary structure of titin highlights the <scene name='78/781193/Hydrophobic_structure_tc_trp/1'><scene name='78/781193/Hydrophobic_structure_tc/1'>polar.</scene> sections of the titin molecule. In this representation, Polar sections of titin are shaded in purple and hydrophobic regions are shaded in grey. The central beta-sandwich structure of the molecule encloses a well defined hydrophobic core. This helps to stabilize the molecule that contains no disulfide bridges and rely solely on hydrogen bonding in the side chains and backbone. Trp34 is also highlighted in this representation to display the central position of the elongated hydrophobic core formed between the two β sheets of the classical Ig folded domain.

•This alternate structure highlights the <scene name='78/781193/Tyr_selection_tc/1'>Tyrosine</scene> involved in activity regulation. Full activation of the protein kinase domain requires both phosphorylation of Tyrosine to prevent it from blocking the catalytic aspartate residue, and binding of the C-terminal regulatory tail of the molecule which results in ATP binding to the kinase.

Sandbox GGC5: Difference between revisions

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@@ Line 44: / Line 44: @@
 •This is the <scene name='78/781193/Titin_rainbow_tc/1'>rainbow</scene> version of the titin molecule. This structure is colored to differentiate each chain, starting with the blue 5' amino end, ending with the red 3' carboxyl end.
-•This secondary structure of titin highlights the <scene name='78/781193/Hydrophobic_structure_tc/1'>polar.</scene> sections of the titin molecule. In this representation, Polar sections of titin are shaded in purple and hydrophobic regions are shaded in grey. The central beta-sandwich structure of the molecule encloses a well defined hydrophobic core. This helps to stabilize the molecule that contains no disulfide bridges and rely solely on hydrogen bonding in the side chains and backbone.
+•This secondary structure of titin highlights the <scene name='78/781193/Hydrophobic_structure_tc_trp/1'><scene name='78/781193/Hydrophobic_structure_tc/1'>polar.</scene> sections of the titin molecule. In this representation, Polar sections of titin are shaded in purple and hydrophobic regions are shaded in grey. The central beta-sandwich structure of the molecule encloses a well defined hydrophobic core. This helps to stabilize the molecule that contains no disulfide bridges and rely solely on hydrogen bonding in the side chains and backbone. Trp34 is also highlighted in this representation to display the central position of the elongated hydrophobic core formed between the two β sheets of the classical Ig folded domain.
 •This alternate structure highlights the <scene name='78/781193/Tyr_selection_tc/1'>Tyrosine</scene> involved in activity regulation. Full activation of the protein kinase domain requires both phosphorylation of Tyrosine to prevent it from blocking the catalytic aspartate residue, and binding of  the C-terminal regulatory tail of the molecule which results in ATP binding to the kinase.