Abstract
Arising from: M. Sadqi, D. Fushman & V. Muñoz Nature 442, 317–321 (2006)10.1038/nature04859; M. Sadqi et al. reply
The folding of small proteins has been assumed to be an all-or-none process that involves high cooperativity within the structure and substantial kinetic-energy barriers. Sadqi et al.1 claim that the small re-engineered protein Naf-BBL unfolds without significant cooperativity or kinetic hindrance, a conclusion that is based on calculation of a broad distribution of midpoint thermal-transition temperatures measured by the nuclear magnetic resonance (NMR) chemical shifts of 158 protons. We find that all of the unprocessed melting curves can be fitted to the same two-state global unfolding when uncertainties in the experimental data are taken into account. We conclude that the authors' melting data for Naf-BBL remain consistent with the all-or-none process.
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References
Sadqi, M., Fushman, D. & Muñoz, V. Nature 442, 317–321 (2006).
Ferguson, N., Schartau, P. J., Sharpe, T. D., Sato, S. & Fersht, A. R. J. Mol. Biol. 344, 295–301 (2004).
Naganathan, A. N., Perez-Jimenez, R., Sanchez-Ruiz, J. M. & Muñoz, V. Biochemistry 44, 7435–7449 (2005).
Dyson, H. J. & Wright, P. E. Adv. Protein Chem. 62, 311–340 (2002).
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Zhou, Z., Bai, Y. Analysis of protein-folding cooperativity. Nature 445, E16–E17 (2007). https://doi.org/10.1038/nature05644
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DOI: https://doi.org/10.1038/nature05644
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