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Folding-Unfolding Transitions in Single Titin Molecules Characterized with Laser Tweezers

Kellermayer, Miklós S. Z., Smith, Steven B., Granzier, Henk L., Bustamante, Carlos·1997·Science

Abstract

Titin, a giant filamentous polypeptide, is believed to play a fundamental role in maintaining sarcomeric structural integrity and developing what is known as passive force in muscle. Measurements of the force required to stretch a single molecule revealed that titin behaves as a highly nonlinear entropic spring. The molecule unfolds in a high-force transition beginning at 20 to 30 piconewtons and refolds in a low-force transition at ∼2.5 piconewtons. A fraction of the molecule (5 to 40 percent) remains permanently unfolded, behaving as a wormlike chain with a persistence length (a measure of the chain’s bending rigidity) of 20 angstroms. Force hysteresis arises from a difference between the unfolding and refolding kinetics of the molecule relative to the stretch and release rates in the experiments, respectively. Scaling the molecular data up to sarcomeric dimensions reproduced many features of the passive force versus extension curve of muscle fibers.

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Metadata

Authors
Kellermayer, M. S. Z., Smith, S. B., Granzier, H. L., & Bustamante, C.
Venue
Science
Published
1997-05-16
Volume
276
Issue
5315
Pages
1112-1116
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2172039086
Cited by
1,217
References
0
FWCI
44.87
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Folding-Unfolding Transitions in Single Titin Molecules Characterized with Laser Tweezers. https://app.cochat.ai/papers/10.1126/science.276.5315.1112
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Kellermayer, M. S. Z., Smith, S. B., Granzier, H. L., & Bustamante, C. (1997). Folding-Unfolding Transitions in Single Titin Molecules Characterized with Laser Tweezers. Science. https://doi.org/10.1126/science.276.5315.1112

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