Hi guys,
I realized that the relax-tighten optimization approach found in most
computational chemistry experiments may be ill-suited for the protein
folding problem. So I'm developing a new merging-tree iterative deepening
search algorithm that will navigate through the protein folding well.
However, this algorithm hinges on one key assumption: there are many initial
pathways in the protein folding landscape with a SIGNIFICANT amount of
pathway convergence as the protein folds. A corollary of this assumption
would be intermediates that result from the merges (nodes), which have the
unique property of resulting from multiple merges and thus would be found in
high frequency no matter how many times you refold a protein.
I was looking through experimental techniques in circular dichroism and NMR,
ideally something that would permit observation of a rapid decrease in
fluctuations of a few, key, residues. Any ideas how I can find these things?
Cheers,
Yutong Zhao
