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Science 16 May 1997:
Vol. 276. no. 5315, pp. 1109 - 1112
DOI: 10.1126/science.276.5315.1109

Reports

Reversible Unfolding of Individual Titin Immunoglobulin Domains by AFM

Matthias Rief, Mathias Gautel, Filipp Oesterhelt, Julio M. Fernandez, Hermann E. Gaub *

Single-molecule atomic force microscopy (AFM) was used to investigate the mechanical properties of titin, the giant sarcomeric protein of striated muscle. Individual titin molecules were repeatedly stretched, and the applied force was recorded as a function of the elongation. At large extensions, the restoring force exhibited a sawtoothlike pattern, with a periodicity that varied between 25 and 28 nanometers. Measurements of recombinant titin immunoglobulin segments of two different lengths exhibited the same pattern and allowed attribution of the discontinuities to the unfolding of individual immunoglobulin domains. The forces required to unfold individual domains ranged from 150 to 300 piconewtons and depended on the pulling speed. Upon relaxation, refolding of immunoglobulin domains was observed.

M. Rief, F. Oesterhelt, H. E. Gaub, Lehrstuhl für Angewandte Physik, Amalienstrasse 54, 80799 München, Germany.
M. Gautel, Biological Structures Division, European Molecular Biology Laboratory, Postfach 102209, 69012 Heidelberg, Germany.
J. M. Fernandez, Department of Physiology and Biophysics, Mayo Clinic, Rochester, MN 55905, USA.
*   To whom correspondence should be addressed.


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