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  • Title: Structural biology: analysis of protein-folding cooperativity.
    Author: Zhou Z, Bai Y.
    Journal: Nature; 2007 Feb 15; 445(7129):E16-7; discussion E17-8. PubMed ID: 17301743.
    Abstract:
    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. 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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