Hello All,
I have a quick question concerning the implications of MD with AMBER.
I am aware of Anfinsen's dogma that the aa sequence can determine the folding pattern of a protein and also of Levinthal's paradox which states that for a polypeptide of length n amino acids, the possible number of folding possibilities is 4^n.
My question then is this - Is it reasonable to state that for a given protein subjected to MD, the number of low energy states that are derived during the simulation can give a relatively small set of possible aa folded states in contradiction to Levinthal's paradox?
I do look forward to your responses and have a great day!
Pat Campbell
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Received on Sun Nov 02 2008 - 05:08:02 PST
