- #1
Bio-student
- 21
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I've been given an 'assignment' of sorts (more of a thought exercise really) to mutate specific amino acid residues in a viral protein (from poliovirus) such that it can catalyse its own cleavage independently of RNA.
I've learned from my own research that the usual cleavage mechanism involves phosphate groups on the RNA backbone coordinating a zinc ion, and positioning it such that it coordinates oxygens in the carbonyl group of the scissile peptide bond, thereby polarising it. Once polarised, I assume the scissile bond is 'activated' for the subsequent steps of cleavage.
I'm really confused as to how to replicate this mechanism in the absence of RNA and would appreciate any pointers (not answers necessarily, just hints, as I am totally lost!) The only vague guidance I've been given is something to do with the torsion angles of the amino acid backbone. Thanks in advance... :)
I've learned from my own research that the usual cleavage mechanism involves phosphate groups on the RNA backbone coordinating a zinc ion, and positioning it such that it coordinates oxygens in the carbonyl group of the scissile peptide bond, thereby polarising it. Once polarised, I assume the scissile bond is 'activated' for the subsequent steps of cleavage.
I'm really confused as to how to replicate this mechanism in the absence of RNA and would appreciate any pointers (not answers necessarily, just hints, as I am totally lost!) The only vague guidance I've been given is something to do with the torsion angles of the amino acid backbone. Thanks in advance... :)