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Comment
. 2015 Dec 15;112(50):E6831-2.
doi: 10.1073/pnas.1517712112. Epub 2015 Nov 24.

Strict experimental evidence that apo-chaperonin GroEL does not accelerate protein folding, although it does accelerate one of its steps

Natalia Y Marchenko  1 , Victor V Marchenkov  1 , Gennady V Semisotnov  1 , Alexei V Finkelstein  2
Affiliations
Comment

Strict experimental evidence that apo-chaperonin GroEL does not accelerate protein folding, although it does accelerate one of its steps

Natalia Y Marchenko et al. Proc Natl Acad Sci U S A. .
No abstract available

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Conflict of interest statement

The authors declare no conflict of interest.

Figures

Fig. 1.
Fig. 1.
A scheme of the protein folding/unfolding (1) with all kinetic constants k and the following from them relative concentrations (in percent) of all of the involved states: F, free folded protein; F-G, chaperonin-bound folded protein; I, free unfolded protein; I-G, chaperonin-bound unfolded protein. Comparison of the underlined rates shows that the entire chaperonin-unassisted folding (I→F) takes less time than only one step I→I-G of the chaperonin-assisted folding.
See this image and copyright information in PMC

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References

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    1. Finkelstein AV. Time to overcome the high, long, and bumpy free energy barrier in a multi-stage process: The generalized steady-state approach. J Phys Chem B. 2015;119(1):158–163. - PubMed
    1. Marchenkov VV, et al. The interaction of the GroEL chaperone with early kinetic intermediates of renaturing proteins inhibits the formation of their native structure. Biophysics. 2004;49(6):888–894. - PubMed

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