Sandbox Reserved 1051: Difference between revisions
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[[Image:Ag85 ebselen.jpg |100 xp|left|thumb|'''Figure 3.''' [http://proteopedia.org/wiki/index.php/4qdu Ag85C-ebselen]: Ebselen covalently binds to Cys209 and forces the otherwise kinked helix α-9 to take on a relaxed conformation, thus allowing movement of the helix and a reduction in enzymatic activity. The native structure is shown in blue, while the modified version is shown in purple, demonstrating a relaxed helix. Ebselen bound Cys209 is shown in green.]] | [[Image:Ag85 ebselen.jpg |100 xp|left|thumb|'''Figure 3.''' [http://proteopedia.org/wiki/index.php/4qdu Ag85C-ebselen]: Ebselen covalently binds to Cys209 and forces the otherwise kinked helix α-9 to take on a relaxed conformation, thus allowing movement of the helix and a reduction in enzymatic activity. The native structure is shown in blue, while the modified version is shown in purple, demonstrating a relaxed helix. Ebselen bound Cys209 is shown in green.]] | ||
[[Image:ebselen pic.jpg |100 xp|left|thumb|'''Figure | [[Image:ebselen pic.jpg |100 xp|left|thumb|'''Figure 5.''' Ebselen.]] | ||
<scene name='69/694218/Ebselen/1'>Ag85C-Ebselen</scene> (Figure 3) is characterized by a covalent bond between [http://en.wikipedia.org/wiki/Ebselen ebselen] and Cys209, thus forcing the otherwise kinked helix α-9 to take on a relaxed conformation (Figure 3). This allows movement of the helix and causes disruption of the hydrogen bonds within the catalytic triad, ultimately inactivating Ag85C.<ref name="Favrot"/> | <scene name='69/694218/Ebselen/1'>Ag85C-Ebselen</scene> (Figure 3) is characterized by a covalent bond between [http://en.wikipedia.org/wiki/Ebselen ebselen] and Cys209, thus forcing the otherwise kinked helix α-9 to take on a relaxed conformation (Figure 3). This allows movement of the helix and causes disruption of the hydrogen bonds within the catalytic triad, ultimately inactivating Ag85C.<ref name="Favrot"/> | ||