The folding cooperativity of a protein is controlled by its chain topology

Elizabeth A. Shank, Ciro Cecconi, Jesse W. Dill, Susan Marqusee () and Carlos Bustamante ()
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Elizabeth A. Shank: University of California, Berkeley, California 94720, USA
Ciro Cecconi: University of California, Berkeley, California 94720, USA
Jesse W. Dill: Jason L. Choy Laboratory of Single Molecule Biophysics, Institute for Quantitative Biosciences, University of California, Berkeley, California 94720, USA
Susan Marqusee: University of California, Berkeley, California 94720, USA
Carlos Bustamante: University of California, Berkeley, California 94720, USA

Nature, 2010, vol. 465, issue 7298, 637-640

Abstract: Into the fold: protein domains reshuffled Protein molecules often include domains that can be distinguished as relatively separate regions in their three-dimensional structure, but how such domains communicate during folding or enzymatic function is largely unclear. Shank et al. have now developed a new technology to study this using single-molecule optical tweezers acting via DNA 'handles' to pull on a protein from different directions while monitoring the energetics of unfolding and refolding events in regions away from those submitted to mechanical forces. Comparing topological variants of a protein — the two-domain protein T4 lysozyme that is a familiar model for folding studies — they then derive new rules of cooperation between sub-domains and suggest how evolution may select reshuffled gene topologies that bypass folding dead-ends.

Date: 2010
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DOI: 10.1038/nature09021

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