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. 2018 Apr 6;293(14):5062. doi: 10.1074/jbc.L118.002358

Comment on the calculations in protein thermodynamics

Jonghoon Kang 1,1, Kyle V Brooks 1
PMCID: PMC5892575  PMID: 29626106

We found a recent paper (1) that would be valuable in the field of protein thermodynamics. However, the paper contains some calculation errors. Here, we discuss the errors. Following the notations in Table 2 of the paper, the ensuing relationship of entropy can be established.

TΔS0Maltose: MBP + TΔS0MBP: sAB-11M in 1 mm maltose = TΔS0MBP: sAB-11M + TΔS0Maltose: MBP in 5-fold molar excess sAB-11M. Plugging the corresponding values reported in Table 2 of the paper to the equation does not satisfy the equality: 10.4 + (−2.0) ≠ 5.6 + 2.0 (in kcal/mol).

Secondly, there are errors made in the calculation of ΔG0 in Table 2. Based on the equation, ΔG0 = ΔH0TΔS0 (2), we found that ΔG0MBP: sAB-11M in 1 mm maltose = −14 − (−2) = −12 kcal/mol, not −11.4 kcal/mol as stated in the paper.ΔG0Maltose: MBP in 5-molar excess of sAB-11M = −8.9 − 2 = −10.9 kcal/mol, not −11.1 kcal/mol. ΔG0Maltose: MBP in 5-molar excess of sAB-P1 = −14 − (−1.0) = −13 kcal/mol, not −12.6 kcal/mol.

The third error we found is with KD for the binding of MBP to sAB-P1 in 1 mm maltose in Table 2: KD = exp (ΔG0/RT) = exp(−11,000 cal/mol × 4.184J/cal/(8.314 J/mol K × 298.15 K)) = 8.6 nm, not 0.9 nm as in the paper. Lastly, Kmal and KsAB in Fig. 5 are 0.83 × 10−6 m and 0.47 × 10−6 m, not 0.83 × 10−3 m and 0.47 × 10−3 m, respectively.

Footnotes

The authors declare that they have no conflicts of interest with the contents of this article.

References

  • 1. Mukherjee S., Griffin D. H., Horn J. R., Rizk S. S., Nocula-Lugowska M., Malmqvist M., Kim S. S., and Kossiakoff A. A. (2018) Engineered synthetic antibodies as probes to quantify the energetic contributions of ligand binding to conformational changes in proteins. J. Biol. Chem. 293, 2815–2828 10.1074/jbc.RA117.000656 [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 2. Chang R. (2000) Physical Chemistry for the Chemical and Biological Sciences. University Science Books, Sausalito, CA [Google Scholar]

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