Persistence length of titin from rabbit skeletal muscles measured with scattering and microrheology techniques

Di Cola, E.; Trinick, J.; Tskhovrebova, A. H.; Dewhurst, C.; Pyckhout-Hintzen, W.; Waigh, T. A.

doi:10.1529/biophysj.104.054908

Journal Article

Persistence length of titin from rabbit skeletal muscles measured with scattering and microrheology techniques

Di Cola, E. ; Waigh, T. A. ; Trinick, J. ; Tskhovrebova, A. H. ; Pyckhout-Hintzen, W.FZJ* ; Dewhurst, C.

2005
Rockefeller Univ. Press New York, NY

Biophysical journal 88, 4095 - 4106 (2005) [10.1529/biophysj.104.054908]

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Please use a persistent id in citations: http://hdl.handle.net/2128/1132 doi:10.1529/biophysj.104.054908

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. Values of persistence length in the range 9-16 nm were found for titin-II, which corresponds to mainly physiologically inelastic A-band part of the protein, and for a proteolytic fragment with 100-nm contour length from the physiologically elastic I-band part. The ratio of the hydrodynamic radius to the static radius of gyration indicates that the proteins obey Gaussian statistics typical of a flexible polymer in a -solvent. Furthermore, measurements of the flexibility as a function of temperature demonstrate that titin-II and the I-band titin fragment experience a similar denaturation process; unfolding begins at 318 K and proceeds in two stages: an initial gradual 50% change in persistence length is followed by a sharp unwinding transition at 338 K. Complementary microrheology (video particle tracking) measurements indicate that the viscoelasticity in dilute solution behaves according to the Flory/Fox model, providing a value of the radius of gyration for titin-II (63 +/- 1 nm) in agreement with static light scattering and small angle neutron scattering results.

Keyword(s): Animals (MeSH) ; Biophysical Phenomena (MeSH) ; Biophysics (MeSH) ; Elasticity (MeSH) ; Light (MeSH) ; Muscle Proteins: chemistry (MeSH) ; Muscle, Skeletal: chemistry (MeSH) ; Neutrons (MeSH) ; Protein Conformation (MeSH) ; Protein Kinases: chemistry (MeSH) ; Rabbits (MeSH) ; Rheology (MeSH) ; Scattering, Radiation (MeSH) ; Temperature (MeSH) ; Muscle Proteins ; connectin ; Protein Kinases ; J