Sandbox Reserved 960: Difference between revisions

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=== Cavity ===

The dynamic structure of the protein is responsible of the ligand’s binding by adjustment of position. The successful delivery of the effector to the receptor relies on this property. The ligand binding pocket consists in a <scene name='60/604479/Cavity/3'>cavity</scene> <ref>PMID: 25337796</ref> formed by the helices H2, H3, H4, H5 and H6 arranged in a globular shape which leads to a clear separation of the ligand from the {{Template:ColorKey_Polar}} environment.

The top of the cavity is not closed and can establish contacts with the solvent. The cavity is prone to accept ligand such as 9-ODA because of its specific composition. Indeed, cavity's components are mainly <scene name='60/604479/~~hydrophobic_residues~~/2'>hydrophobic and aromatic</scene> <ref>PMID: 14594955</ref>.They consequently interact with the ligand's {{Template:ColorKey_Hydrophobic}} carbon chain and are localized on the internal face of the helix.Thus, it implies that these residues respect a regular distance pattern in the primary structure of the AmelASP1.

The top of the cavity is not closed and can establish contacts with the solvent. The cavity is prone to accept ligand such as 9-ODA because of its specific composition. Indeed, cavity's components are mainly <scene name='60/604479/Hydrophobic_residues/2'>hydrophobic and aromatic</scene> <ref>PMID: 14594955</ref>.They consequently interact with the ligand's {{Template:ColorKey_Hydrophobic}} carbon chain and are localized on the internal face of the helix.Thus, it implies that these residues respect a regular distance pattern in the primary structure of the AmelASP1.

=== pH influence ===

Sandbox Reserved 960: Difference between revisions

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@@ Line 48: / Line 48: @@
 === Cavity ===
 The dynamic structure of the protein is responsible of the ligand’s binding by adjustment of position. The successful delivery of the effector to the receptor relies on this property. The ligand binding pocket consists in a <scene name='60/604479/Cavity/3'>cavity</scene> <ref>PMID: 25337796</ref> formed by the helices H2, H3, H4, H5 and H6 arranged in a globular shape which leads to a clear separation of the ligand from the {{Template:ColorKey_Polar}} environment.
-The top of the cavity is not closed and can establish contacts with the solvent. The cavity is prone to accept ligand such as 9-ODA because of its specific composition. Indeed, cavity's components are mainly <scene name='60/604479/hydrophobic_residues/2'>hydrophobic and aromatic</scene> <ref>PMID: 14594955</ref>.They consequently interact with the ligand's {{Template:ColorKey_Hydrophobic}} carbon chain and are localized on the internal face of the helix.Thus, it implies that these residues respect a regular distance pattern in the primary structure of the AmelASP1.
+The top of the cavity is not closed and can establish contacts with the solvent. The cavity is prone to accept ligand such as 9-ODA because of its specific composition. Indeed, cavity's components are mainly <scene name='60/604479/Hydrophobic_residues/2'>hydrophobic and aromatic</scene> <ref>PMID: 14594955</ref>.They consequently interact with the ligand's {{Template:ColorKey_Hydrophobic}} carbon chain and are localized on the internal face of the helix.Thus, it implies that these residues respect a regular distance pattern in the primary structure of the AmelASP1.
 === pH influence ===