Single-molecule fluorescence reveals sequence-specific misfolding in multidomain proteins

Madeleine B. Borgia, Alessandro Borgia, Robert B. Best, Annette Steward, Daniel Nettels, Bengt Wunderlich, Benjamin Schuler () and Jane Clarke ()
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Madeleine B. Borgia: University of Cambridge Chemical Laboratory, Lensfield Road, Cambridge CB2 1EW, UK
Alessandro Borgia: Biochemisches Institut, Universität Zürich, Winterthurerstrasse 190, 8057 Zürich, Switzerland
Robert B. Best: University of Cambridge Chemical Laboratory, Lensfield Road, Cambridge CB2 1EW, UK
Annette Steward: University of Cambridge Chemical Laboratory, Lensfield Road, Cambridge CB2 1EW, UK
Daniel Nettels: Biochemisches Institut, Universität Zürich, Winterthurerstrasse 190, 8057 Zürich, Switzerland
Bengt Wunderlich: Biochemisches Institut, Universität Zürich, Winterthurerstrasse 190, 8057 Zürich, Switzerland
Benjamin Schuler: Biochemisches Institut, Universität Zürich, Winterthurerstrasse 190, 8057 Zürich, Switzerland
Jane Clarke: University of Cambridge Chemical Laboratory, Lensfield Road, Cambridge CB2 1EW, UK

Nature, 2011, vol. 474, issue 7353, 662-665

Abstract: When protein folding goes awry Three in four human proteins have multiple domains, and the tendency of these proteins to aggregate increases with amino-acid sequence similarity. Single-molecule biophysics experiments now show that the misfolding is caused by strand-swapping between adjacent domains, and that diversification of sequence between neighbouring domains lowers the probability of misfolding. The work also indicates that such misfolding events are under kinetic rather than thermodynamic control. Because domain-swapped protein species have been implicated in various misfolding diseases, prevention of inter-domain misfolding may be protective against aggregation disorders.

Date: 2011
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DOI: 10.1038/nature10099

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