Abstract
We study the critical relaxation of the helix-coil transition in all-atom models of polyalanine chains. We show that at the critical temperature the decay of a completely helical conformation can be described by scaling relations that allow us estimating the pertinent critical exponents. The present approach opens a new way for characterizing transitions in proteins and may lead to a better understanding of their folding mechanism. An application of the technique to the 34-residue human parathyroid fragment PTH(1-34) supports universality of the helix-coil transition in homopolymers and (helical) proteins.
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