Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Titin folding energy and elasticity

A Soteriou1, A Clarke, S Martin

  • 1Department of Veterinary Medicine, Bristol University, Langford, U.K.

Proceedings. Biological Sciences
|November 22, 1993
PubMed
Summary

The giant protein titin provides muscle elasticity through domain unfolding. Its I-band region undergoes two cooperative unfolding transitions, explaining its extensibility in muscle fibers.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

The governance of surgical innovation in the UK National Health Service.

The British journal of surgery·2026
Same author

The effects of simultaneous isometric and eccentric- or concentric-biased exercise on cardiovascular and muscular health of young individuals.

European journal of applied physiology·2026
Same author

The distribution of healthcare workforces relative to population ill health in England: Repeated cross-sectional analysis of Census data 2001-2021.

Public health·2025
Same author

Prevalence of transthyretin cardiac amyloidosis in undifferentiated heart failure with preserved ejection fraction.

ESC heart failure·2024
Same author

The inflexible mind: A critical factor in understanding and addressing COVID-19 vaccine hesitancy.

Journal of psychiatric research·2024
Same author

An outbreak of SARS-CoV-2 in a public-facing office in England.

Occupational medicine (Oxford, England)·2023

Area of Science:

  • Muscle physiology
  • Protein biophysics
  • Biochemistry

Background:

  • The giant protein titin is crucial for passive muscle elasticity and myofibril structure.
  • The I-band region of titin can extend reversibly up to fourfold, but its molecular mechanism remains unclear.
  • This extensibility is hypothesized to involve the unfolding of titin's protein domains.

Purpose of the Study:

  • To investigate the equilibrium unfolding of titin molecules.
  • To elucidate the molecular mechanisms underlying titin's elasticity.
  • To determine the thermodynamic properties of titin domain unfolding.

Main Methods:

  • Studied titin from rabbit skeletal muscle in vitro.
  • Utilized fluorescence spectroscopy to monitor unfolding.
  • Employed circular dichroism spectroscopy for structural analysis.
  • Applied guanidinium chloride as a denaturant to induce unfolding.

Main Results:

  • Observed two distinct cooperative unfolding transitions for titin.
  • The second transition likely corresponds to the complete unfolding of immunoglobulin and fibronectin-like domains.
  • The free energy of the second transition closely matches the energy required for in situ titin extension.

Conclusions:

  • Titin's elasticity arises from the cooperative unfolding of its immunoglobulin and fibronectin-like domains.
  • The observed unfolding transitions provide a molecular explanation for titin's remarkable extensibility.
  • The study links in vitro unfolding thermodynamics to in situ mechanical function of titin.

Related Experiment Videos