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Comment
. 2009 Jul 21;106(29):11823-4.
doi: 10.1073/pnas.0906228106. Epub 2009 Jul 15.

Protein folding roller coaster, one molecule at a time

Affiliations
Comment

Protein folding roller coaster, one molecule at a time

Eugene Shakhnovich. Proc Natl Acad Sci U S A. .
No abstract available

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Conflict of interest statement

The author declares no conflict of interest.

Figures

Fig. 1.
Fig. 1.
Cooperative protein folding. Most of the time the chain spends in the unfolded ensemble (corresponding to the free-energy minimum on the right, until a fluctuation brings it rapidly to the top of the free-energy barrier from which it has 50% chance (pfold) to proceed quickly to the native state (on the left) or to unfold back. The reaction coordinate shown here is hypothetical. The mere existence of a 1D order parameter suitable for the description of protein folding kinetics in terms of a 1D barrier crossing is a matter of lively debate in the field.
Fig. 2.
Fig. 2.
Folding scenario of protein G derived from all-atom Monte Carlo simulations (5). Several pathways of unequal probability lead to the transition-state ensemble where the folding nucleus comprised of few hydrophobic amino acids is formed. Reprinted from ref. .

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