Levinthal's Paradox

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Peter Foster, In progress Fall 2011

Entry needed.

It is well known that proteins in solution can reliably fold from a random coil to a unique native conformation on a biologically relavent timescale. Levinthal's paradox is an apparent contradiction between the number of possible conformations for a protein chain and the fact that proteins can fold to their native conformation quickly (less than a second). In the proceedings where Levinthal first mentioned the paradox that bears his name, he estimates that for a protein there are 10300 possible conformations. Using the amount of time it actually takes for a protein to fold to its native conformation and assuming the minimal amount of time to sample different conformations, the protein would only be able to sample ~108 different conformations if the protein sampled the conformation space randomly.


[1] Levinthal's Paradox

Keyword in references:

G. Lois, J. Blawzdziewicz, and C. S. O'Hern, "Protein folding on rugged energy landscapes: Conformational diffusion on fractal networks", Phys. Rev. E 81 (2010) 051907

Reliable Protein Folding on Complex Energy Landscapes: The Free Energy Reaction Path