Sandbox Reserved 1051: Difference between revisions
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===Ag85C-Hg=== | ===Ag85C-Hg=== | ||
[[Image:Ag85C Hg.jpg |100 xp|left|thumb|'''Figure 4.''' [http://proteopedia.org/wiki/index.php/4qdo Ag85C-Hg]: A modification of Ag85C generated with the addition of p-chloromercuribenzoic acid compared to the native structure. This modified enzyme lacks a hydrogen bond between Glu228 and His260, which relaxes the kink normally found in the native structure and inhibits the active site.]] | [[Image:Ag85C Hg.jpg |100 xp|left|thumb|'''Figure 4.''' [http://proteopedia.org/wiki/index.php/4qdo Ag85C-Hg]: A modification of Ag85C generated with the addition of p-chloromercuribenzoic acid compared to the native structure. This modified enzyme lacks a hydrogen bond between Glu228 and His260, which relaxes the kink normally found in the native structure and inhibits the active site. Glu228 and His260 are shown in red. The addition of p-chloromercuribenzoic acid disrupts the hydrogen bond between the two resides, causing a change in the helix conformation of this modified structure. The native structure is shown in green and the relaxed, modified structure is shown in blue.]] | ||
The mutant [http://proteopedia.org/wiki/index.php/4qdo Ag85C-Hg] (Figure 4) is generated with the addition of [http://en.wikipedia.org/wiki/4-Chloromercuribenzoic_acid p-chloromercuribenzoic acid], the side chain of the complex is disordered due to a lack of hydrogen bonds between Glu228 and His260. Similar to what is observed in Ag85C-ebselen, the alteration in <scene name='69/694218/Ag85c-hg/1'>Ag85C-Hg</scene> relaxes the kinked helix α-9 found in the native structure of the enzyme, thus inhibiting the active site. The ultimate effect is a decrease to only 60% of the normal enzymatic function of Ag85C.<ref name="Favrot"/> | The mutant [http://proteopedia.org/wiki/index.php/4qdo Ag85C-Hg] (Figure 4) is generated with the addition of [http://en.wikipedia.org/wiki/4-Chloromercuribenzoic_acid p-chloromercuribenzoic acid], the side chain of the complex is disordered due to a lack of hydrogen bonds between Glu228 and His260. Similar to what is observed in Ag85C-ebselen, the alteration in <scene name='69/694218/Ag85c-hg/1'>Ag85C-Hg</scene> relaxes the kinked helix α-9 found in the native structure of the enzyme, thus inhibiting the active site. The ultimate effect is a decrease to only 60% of the normal enzymatic function of Ag85C.<ref name="Favrot"/> | ||
