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Comment
. 2004 Dec 14;101(50):17327-8.
doi: 10.1073/pnas.0407863101. Epub 2004 Dec 6.

Phi value versus psi analysis

Alan R Fersht  1
Affiliations
Comment

Phi value versus psi analysis

Alan R Fersht. Proc Natl Acad Sci U S A. .
No abstract available

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Figures

Fig. 1.
Fig. 1.
The effects of metal binding on protein folding. (Left) Thermodynamic cycle for rapid distribution of M2+ ion (M) between denatured (D) and native (N) states. (Right) Simulated plots for the cycle of ΔΔG‡ (= RTln((kf(M)[M2+]/kf(0) + KMD)/(KMD + [M2+]))) vs. ΔΔG0 (= RTln((kf(M)[M2+]/kf(0) + KMD)/(KMD + [M2+])) – RTln((ku(M)[M2+]/ku(0) + KMN)/(KMN + [M2+]))). From left to right, A, KMD = 500 μM, KMN = 50 μM, kf(0) = 1,000/s, kf(M) = 3,160/s, ku(0) = 100/s, ku(M) = 31.6; B, KMD = 500 μM, KMN = 5 μM, kf(0) = 1,000/s, kf(M) = 10,000/s, ku(0) = 100/s, ku(M) = 10/s; C, KMD = 500 μM, KMN = 1 μM, kf(0) = 1,000/s, kf(M) = 22,360/s, ku(0) = 100/s, ku(M) = 4.47. These plots all are constructed to have 50% of the metal binding energy present in the transition state (f = 0.5) for two simple parallel pathways without any heterogeneity of the transition state in the absence of M2+. The three plots fit with 100% precision to the proposed ψ plot (Eq. 1) with f values of 1.0 for each and kabs/kpres(0) of 3.167, 10, and 22.36, respectively, and corresponding values of ψ0 of 0.24, 0.09, and 0.04.
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References

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