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Originally published as Biophys J. BioFAST on December 30, 2005.
doi:10.1529/biophysj.105.078436
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Biophysical Journal 90:L30-L32 (2006)
© 2006 The Biophysical Society

Stepwise Unfolding of Ankyrin Repeats in a Single Protein Revealed by Atomic Force Microscopy

Lewyn Li *, Svava Wetzel {dagger}, Andreas Plückthun {dagger} and Julio M. Fernandez *

* Department of Biological Sciences, Columbia University, New York, New York 10027; and {dagger} Biochemisches Institut, Universität Zürich, CH-8057 Zürich, Switzerland

Correspondence: Address reprint requests and inquiries to Julio M. Fernandez, Tel.: 212-854-9141; Fax: 212-854-4619; E-mail: jfernandez{at}columbia.edu.

Using single-molecule atomic force microscopy, we find that a protein consisting of six identical ankyrin repeat units flanked by N- and C-terminal modules (N6C) unfolds in a stepwise, unit-by-unit fashion under a mechanical force. Stretching a N6C molecule results in a sawtooth pattern fingerprint, with as many as six peaks separated by ~10 nm and an average unfolding force of 50 ± 20 pN. Our results demonstrate that a stretching force can unfold multiple repeat units individually in a single protein molecule, despite extensive hydrophobic interactions between adjacent units.




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