Bioseparations Principles And Techniques By B Sivasankar Ebook Free Download
Q:
Why did this accepted answer get deleted?
I was browsing my profile and saw this question: Where is Snow Crash set in our world?
This question had a good answer, but two people upvoted the answer, making it community wiki.
However, someone flagged the answer because it was community wiki, and it was deleted. This flag was rejected as invalid, and the community wiki mark was removed. The question’s owner decided to delete the answer.
When I visited the question to see why it was deleted, I didn’t see any reason why it was deleted. That is, I don’t know what the community’s reason was, nor do I know which users voted to delete it.
Can the question’s owner comment on why it was deleted, or can we request that the owner answer why it was deleted?
A:
I deleted it for the same reason. Once a user is trusted enough to add their own answer (via reputation gain), and then accept an answer, it should be allowed to become a CW community-wiki answer instead.
Answer became community wiki, then that went away. The editor of that post doesn’t have the privilege to edit it back to community wiki, so it wouldn’t have been a great use of time for them to go and make it so.
I suspect that the user flagged the answer to get it removed so they could add their own answer and then accept that one.
As you can’t flag your own deleted answer, I can’t comment on why it was deleted.
A new, sensitive assay for dimerization of the prion protein.
The host-encoded prion protein (PrP), is involved in a diverse set of neurodegenerative pathologies. Despite its abundance, the prion-like protein aggregation process responsible for these illnesses is not fully understood. PrP is an amphipathic molecule, existing in an oligomeric state. A common endpoint used to evaluate the success of prion bioassays involves the detection of PrP(Sc), the disease-specific insoluble protein aggregates found in prion-infected brain tissue. Unfortunately, this indirect method is time-consuming and requires animals for its implementation, making it less practical for biochemical studies. We have developed a direct biochemical assay for dimerization of the full-length human prion protein. Using synthetic peptide sequences flanking the predicted PrP dimerization domain, we designed and screened a pept
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