Sandbox Reserved 390: Difference between revisions
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===Mutation of Glycine at position 465=== | ===Mutation of Glycine at position 465=== | ||
According to earlier experiments, the glycine at position 465 in this structure is proposed to lie very close to the cleavage site 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 | According to earlier experiments, the glycine at position 465 in this structure is proposed to lie very close to the cleavage site 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 site). | ||
[[Image:ASP 465.jpg|thumb|right|500 px|Aspartic Acid at position 465]] | [[Image:ASP 465.jpg|thumb|right|500 px|Aspartic Acid at position 465]] | ||