Sandbox Reserved 830: Difference between revisions

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Helices A and C have breaks in the hydrogen-bonding pattern of their structure, forming tight substitute hydrogen bonds with water molecules. Indeed, it results in a kink in helix A (<scene name='56/568028/Kink_helixa/1'>and slightly in helix C between residues Gln112 and Pro116</scene>) induced by a disruption in the helical conformation, due to the Gln25 and Leu30 hydrogen bonds with four water molecules. Helix A residues between Thr27 and Ile37 take on a ~~310~~ helix conformation. With this curved structure, helices A and C enhance the compaction of the A-D and B-C parallel helix pairs, causing the core of OSM to be isolated from the solvent.

Helices A and C have breaks in the hydrogen-bonding pattern of their structure, forming tight substitute hydrogen bonds with water molecules. Indeed, it results in a kink in helix A (<scene name='56/568028/Kink_helixa/1'>and slightly in helix C between residues Gln112 and Pro116</scene>) induced by a disruption in the helical conformation, due to the Gln25 and Leu30 hydrogen bonds with four water molecules. <scene name='56/568028/Oncostatin_helix_310/1'>Helix A residues between Thr27 and Ile37</scene> take on a 3<sub>10</sub> helix conformation. With this curved structure, helices A and C enhance the compaction of the A-D and B-C parallel helix pairs, causing the core of OSM to be isolated from the solvent.

This core is composed of two aromatic stacking groups, Phe56, Tyr, 173, Phe169 and Phe176 on one hand, and Phe170, Phe185 and Trp187 on the other hand. All these aromatic residues belong to helix D, except Phe56 (AB loop) and Phe70 (Helix B), highlighting the hydrophobicity of helix D.

Sandbox Reserved 830: Difference between revisions

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Revision as of 14:24, 9 January 2014 view source Pierre-Yves Mocaer (talk \| contribs) 210 edits No edit summary ← Older edit		Revision as of 14:35, 9 January 2014 view source Pierre-Yves Mocaer (talk \| contribs) 210 edits No edit summary Newer edit →
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	Helices A and C have breaks in the hydrogen-bonding pattern of their structure, forming tight substitute hydrogen bonds with water molecules. Indeed, it results in a kink in helix A (<scene name='56/568028/Kink_helixa/1'>and slightly in helix C between residues Gln112 and Pro116</scene>) induced by a disruption in the helical conformation, due to the Gln25 and Leu30 hydrogen bonds with four water molecules. Helix A residues between Thr27 and Ile37 take on a ~~310~~ helix conformation. With this curved structure, helices A and C enhance the compaction of the A-D and B-C parallel helix pairs, causing the core of OSM to be isolated from the solvent.		Helices A and C have breaks in the hydrogen-bonding pattern of their structure, forming tight substitute hydrogen bonds with water molecules. Indeed, it results in a kink in helix A (<scene name='56/568028/Kink_helixa/1'>and slightly in helix C between residues Gln112 and Pro116</scene>) induced by a disruption in the helical conformation, due to the Gln25 and Leu30 hydrogen bonds with four water molecules. <scene name='56/568028/Oncostatin_helix_310/1'>Helix A residues between Thr27 and Ile37</scene> take on a 3<sub>10</sub> helix conformation. With this curved structure, helices A and C enhance the compaction of the A-D and B-C parallel helix pairs, causing the core of OSM to be isolated from the solvent.

	This core is composed of two aromatic stacking groups, Phe56, Tyr, 173, Phe169 and Phe176 on one hand, and Phe170, Phe185 and Trp187 on the other hand. All these aromatic residues belong to helix D, except Phe56 (AB loop) and Phe70 (Helix B), highlighting the hydrophobicity of helix D.		This core is composed of two aromatic stacking groups, Phe56, Tyr, 173, Phe169 and Phe176 on one hand, and Phe170, Phe185 and Trp187 on the other hand. All these aromatic residues belong to helix D, except Phe56 (AB loop) and Phe70 (Helix B), highlighting the hydrophobicity of helix D.