User:Erin May/Sandbox 1: Difference between revisions

Line 69:

The following interactions and residue switching portray possible catalytic sites:

Residues 129, 200, and 164 to 170 are shown to exist right at the dimer interfaces (as noted in the previous structures). The location of these residues within the dimer indicates that their key operation is found somewhere in the dimerization process.

Residues 129, 200, and 164 to 170 are shown to exist right at the dimer interfaces (as noted in the previous structures). The location of these residues within the dimer indicates that their key operation is found somewhere in the dimerization process. <ref name="Zhang">PMID:10954699</ref><ref name="Knaus">PMID:11524679</ref>

Helix 1 (Ser 143−Tyr 157) exists at the <scene name='User:Erin_May/Sandbox_1/Nonpolar_at_dimer_interface/2'>dimer interface</scene>. Many nonpolar residues form Van der Waals attractions. Acidic and mostly negative residues are shown in blue. Basic and mostly positive residues are shown in red. The interactions between these also stabilize the dimer interface.

Helix 2 (Asn 171−Thr 188) is <scene name='User:Erin_May/Sandbox_1/Helix_2_with_helix_3/1'>linked</scene> to the C-terminal helix 3 (Thr 199−Tyr 225). Van der Waals forces are here between such nonpolar residues as valine, isoleucene, and nonpolar sections as histadine, methionine, and glutamic acid.<ref name="Knaus">PMID:11524679</ref>

Helix 2 (Asn 171−Thr 188) is <scene name='User:Erin_May/Sandbox_1/Helix_2_with_helix_3/1'>linked</scene> to the C-terminal helix 3 (Thr 199−Tyr 225). Van der Waals forces are here between such nonpolar residues as valine, isoleucene, and nonpolar sections as histadine, methionine, and glutamic acid.<ref name="Knaus">PMID:11524679</ref><ref name="Zhang">PMID:10954699</ref>

The <scene name='User:Erin_May/Sandbox_1/Switch_region/1'>switch region</scene> (residues 189-198) is where the actual unfolding has taken place.

User:Erin May/Sandbox 1: Difference between revisions

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@@ Line 69: / Line 69: @@
 The following interactions and residue switching portray possible catalytic sites:
-Residues 129, 200, and 164 to 170 are shown to exist right at the dimer interfaces (as noted in the previous structures). The location of these residues within the dimer indicates that their key operation is found somewhere in the dimerization process.
+Residues 129, 200, and 164 to 170 are shown to exist right at the dimer interfaces (as noted in the previous structures). The location of these residues within the dimer indicates that their key operation is found somewhere in the dimerization process. <ref name="Zhang">PMID:10954699</ref><ref name="Knaus">PMID:11524679</ref>
 Helix 1 (Ser 143−Tyr 157) exists at the <scene name='User:Erin_May/Sandbox_1/Nonpolar_at_dimer_interface/2'>dimer interface</scene>. Many nonpolar residues form Van der Waals attractions. Acidic and mostly negative residues are shown in blue. Basic and mostly positive residues are shown in red. The interactions between these also stabilize the dimer interface.
-Helix 2 (Asn 171−Thr 188) is <scene name='User:Erin_May/Sandbox_1/Helix_2_with_helix_3/1'>linked</scene> to the C-terminal helix 3 (Thr 199−Tyr 225). Van der Waals forces are here between such nonpolar residues  as valine, isoleucene, and nonpolar sections as histadine, methionine, and glutamic acid.<ref name="Knaus">PMID:11524679</ref>
+Helix 2 (Asn 171−Thr 188) is <scene name='User:Erin_May/Sandbox_1/Helix_2_with_helix_3/1'>linked</scene> to the C-terminal helix 3 (Thr 199−Tyr 225). Van der Waals forces are here between such nonpolar residues  as valine, isoleucene, and nonpolar sections as histadine, methionine, and glutamic acid.<ref name="Knaus">PMID:11524679</ref><ref name="Zhang">PMID:10954699</ref>
 The <scene name='User:Erin_May/Sandbox_1/Switch_region/1'>switch region</scene> (residues 189-198) is where the actual unfolding has taken place.