Explanation of a tertiary structure

Flip Hoedemaeker fhoedem at oci.utoronto.ca
Tue Sep 26 16:46:04 EST 1995

Nicely said Shaun, maybe you have to add that all these energetically favorable 
interactions are needed to compensate for the loss in entropy. In an unfolded
state, the polypeptide chain can wiggle about freely, but its movements are
severly restricted upon folding. If you add up all the favorable and
unfavorable aspects of being folded as a protein, you will find that the
difference is very small.(about 5%?)

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