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Biophys. J. BioFAST: First Published March 25, 2005. doi:10.1529/biophysj.104.054908
© 2005 by the Biophysical Society.

A more recent version of this article appeared on June 1, 2005.
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MUSCLE AND CONTRACTILITY

Persistence Length of Titin from Rabbit Skeletal Muscles Measured with Scattering and Microrheology Techniques

Emanuela Di Cola 1, Thomas Waigh 1*, John Trinick 1, Larissa Tskhovrebova 1, Ahmed Houmeida 1, Wim Pyckhout-Hintzen 2 and Charles Dewhurst 3

1 University of Leeds
2 Julich facility
3 ILL

* To whom correspondence should be addressed. E-mail: t.a.waigh{at}leeds.ac.uk.

Submitted on October 21, 2004
Revised on January 7, 2005
Accepted on 8 March 2005


  Abstract
The persistence length of titin from rabbit skeletal muscles was measured using a combination of static and dynamic light scattering, and neutron small angle scattering. A persistence length in the range of 9-16 nm was found for the protein and an isolated proteolytical fragment of 100 nm contour length. The ratio of the hydrodynamic radius to the static radius of gyration indicates that the protein obeys Gaussian statistics typical of a flexible polymer in a theta solvent. Furthermore, measurements of the chains' flexibility as a function of temperature demonstrate that titin and the fragment experience a similar denaturation process, unfolding begins at 318K in two stages; an initial gradual 50% change in persistence length, followed by a sharp unwinding transition at 338K. Complementary microrheology (video particle tracking) measurements indicate that the chains' viscoelasticity in dilute solution behaves according to the Flory/Fox model, providing a value of the radius of gyration (63 nm) in agreement with SLS and SANS results.

Key Words: Light Scattering, Microrheology, Muscle, Neutrons, Polyampholyte, Titin




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E. von Castelmur, M. Marino, D. I. Svergun, L. Kreplak, Z. Ucurum-Fotiadis, P. V. Konarev, A. Urzhumtsev, D. Labeit, S. Labeit, and O. Mayans
A regular pattern of Ig super-motifs defines segmental flexibility as the elastic mechanism of the titin chain
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[Abstract] [Full Text] [PDF]


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Copyright © 2005 by the Biophysical Society.