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Science 16 May 1997: Vol. 276. no. 5315, pp. 1109 - 1112 DOI: 10.1126/science.276.5315.1109
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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.
Read the Full Text
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- I-Band Titin in Cardiac Muscle Is a Three-Element Molecular Spring and Is Critical for Maintaining Thin Filament Structure.
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- Probing Nanometer Structures with Atomic Force Microscopy.
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Physiology
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