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Brief Communication Arising
Nature 445, E16-E17 (15 February 2007) | doi:10.1038/nature05644; Published online 14 February 2007
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Postdoctoral Associate in Enzyme Biochemistry
- Cornell University
- Ithaca, NY
Tenure Professor for Bone and Skeleton Research
- Westfalian Wilhelms-University Munster, Germany
- Munster Germany
Structural Biology: Analysis of protein-folding cooperativity
Abstract
Arising from: M. Sadqi, D. Fushman & V. Muñoz Nature 442, 317–321 (2006); 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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