Stepwise Unfolding of Titin under Force-Clamp Atomic Force Microscopy

Here we demonstrate the implementation of a single-molecule force clamp adapted for use with an atomic force microscope. We show that under force-clamp conditions, an engineered titin protein elongates in steps because of the unfolding of its modules and that the waiting times to unfold are exponent...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 2001-01, Vol.98 (2), p.468-472
Main Authors: Oberhauser, Andres F., Hansma, Paul K., Carrion-Vazquez, Mariano, Fernandez, Julio M.
Format: Article
Language:English
Subjects:
Animals
Atoms & subatomic particles
Biological Sciences
Cantilevers
Cattle
Connectin
Error signals
Extracellular matrix
Humans
Kinetics
Micromanipulation - instrumentation
Microscopes
Microscopy, Atomic Force
Modeling
Molecules
Muscle Proteins - ultrastructure
Myocardium - chemistry
Polymers
Polyproteins
Protein Engineering
Protein Folding
Protein Kinases - ultrastructure
Proteins
Stress, Mechanical
Time dependence
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Summary:Here we demonstrate the implementation of a single-molecule force clamp adapted for use with an atomic force microscope. We show that under force-clamp conditions, an engineered titin protein elongates in steps because of the unfolding of its modules and that the waiting times to unfold are exponentially distributed. Force-clamp measurements directly measure the force dependence of the unfolding probability and readily captures the different mechanical stability of the I27 and I28 modules of human cardiac titin. Force-clamp spectroscopy promises to be a direct way to probe the mechanical stability of elastic proteins such as those found in muscle, the extracellular matrix, and cell adhesion.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.021321798