User:Youngsen Jeng: Difference between revisions

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Structural stabilization of Glutamine Synthetase by divalent cations, especially by the n1 ion<'''Insert wiki here'''>, has been ascribed to the attraction of their positive charges to the negative charges of glutamate and ATP and of their ligands<'''Insert wiki here'''> (Liaw et al., 1993~).

The structure of the dodecamer exposes several alpha loops which are important in stabilizing quaternary structure of Glutamine Synthetase. One beta loop consists of hydrophilic residues 156-173,<insert wiki> projects into the central channel of the dodecamer. Another beta loop is the ~~adenylylation~~ loop<insert wiki>, so called because it contains tyrosyine residue 397 which is covalently modified by addition of AMP. The amino group of glutamate shifts the Asn-264 loop, helping Ser-53P, on the Asp-50P loop, to stabilize the flap<insert wiki>.downward extension of the two-stranded beta sheet whose strands are connected by the "Trp 57 loop."<insert wiki> These two strands complete the cylindrical active site of the neighboring subunit.(This neighbor is the one clockwise to the subunit, when the molecule is viewed down the 6-fold axis. That is, the Trp-57 loop of subunit F of completes the active site of subunit A)

The structure of the dodecamer exposes several alpha loops which are important in stabilizing quaternary structure of Glutamine Synthetase. One beta loop consists of hydrophilic residues 156-173,<insert wiki> projects into the central channel of the dodecamer. Another beta loop is the <scene name='User:Youngsen_Jeng/Beta_loop_with_tyr_397/1'>adenylation loop</scene><insert wiki>, so called because it contains tyrosyine residue 397 which is covalently modified by addition of AMP. The amino group of glutamate shifts the Asn-264 loop, helping Ser-53P, on the Asp-50P loop, to stabilize the flap<insert wiki>.

=References=

User:Youngsen Jeng: Difference between revisions

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@@ Line 22: / Line 22: @@
 Structural stabilization of Glutamine Synthetase by divalent cations, especially by the n1 ion<'''Insert wiki here'''>, has been ascribed to the attraction of their positive charges to the negative charges of glutamate and ATP and of their ligands<'''Insert wiki here'''> (Liaw et al., 1993~).
-The structure of the dodecamer exposes several alpha loops which are important in stabilizing quaternary structure of Glutamine Synthetase. One beta loop consists of hydrophilic residues 156-173,<insert wiki> projects into the central channel of the dodecamer. Another beta loop is the adenylylation loop<insert wiki>, so called because it contains tyrosyine residue 397 which is covalently modified by addition of AMP. The amino group of glutamate shifts the Asn-264 loop, helping Ser-53P, on the Asp-50P loop, to stabilize the flap<insert wiki>.downward extension of the two-stranded beta sheet whose strands are connected by the "Trp 57 loop."<insert wiki> These two strands complete the cylindrical active site of the neighboring subunit.(This neighbor is the one clockwise to the subunit, when the molecule is viewed down the 6-fold axis. That is, the Trp-57 loop of subunit F of completes the active site of subunit A)
+The structure of the dodecamer exposes several alpha loops which are important in stabilizing quaternary structure of Glutamine Synthetase. One beta loop consists of hydrophilic residues 156-173,<insert wiki> projects into the central channel of the dodecamer. Another beta loop is the <scene name='User:Youngsen_Jeng/Beta_loop_with_tyr_397/1'>adenylation loop</scene><insert wiki>, so called because it contains tyrosyine residue 397 which is covalently modified by addition of AMP. The amino group of glutamate shifts the Asn-264 loop, helping Ser-53P, on the Asp-50P loop, to stabilize the flap<insert wiki>.
 =References=
 <references/>