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

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.

journal_name

Biophys J

journal_title

Biophysical journal

authors

Di Cola E,Waigh TA,Trinick J,Tskhovrebova L,Houmeida A,Pyckhout-Hintzen W,Dewhurst C

doi

10.1529/biophysj.104.054908

subject

Has Abstract

pub_date

2005-06-01 00:00:00

pages

4095-106

issue

6

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(05)73460-3

journal_volume

88

pub_type

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