Sandbox Reserved 390: Difference between revisions

@@ Line 27: / Line 27: @@
 ===Mutation of Glycine at position 465===
-According to earlier experiment, the glycine at position 465 in this structure is proposed to lies very close to the “area binding the gate helix” and it’s is therefore expected to be involved in ATP hydrolysis. So the change of residue 465 from glycine to a more negatively charged (aspartic acid) is determined to create some localized hydrogen bonding at the backbone that can potentially alter the conformation of the enzyme (this change is determined to alter the charge interactions involved in binding of the gate helix).
+According to earlier experiments, the glycine at position 465 in this structure is proposed to lie very close to the “area binding the gate helix” and it’s is therefore expected to be involved in ATP hydrolysis. So the change of residue 465 from glycine to a more negatively charged (aspartic acid) is determined to create some localized hydrogen bonding at the backbone that can potentially alter the conformation of the enzyme (this change is determined to alter the charge interactions involved in binding of the gate helix).
 <scene name='Sandbox_Reserved_390/Top/20'>TextToBeDisplayed</scene>

Navigation menu