Analysis of protein-folding cooperativity

Zheng Zhou () and Yawen Bai ()
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Zheng Zhou: Laboratory of Biochemistry and Molecular Biology, Center for Cancer Research, NCI, NIH, Building 37, Room 6114E
Yawen Bai: Laboratory of Biochemistry and Molecular Biology, Center for Cancer Research, NCI, NIH, Building 37, Room 6114E

Nature, 2007, vol. 445, issue 7129, E16-E17

Abstract: 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.

Date: 2007
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DOI: 10.1038/nature05644

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