Characterization of beta-connectin (titin 2) from striated muscle by dynamic light scattering.

Abstract:

:Connectin (titin) is a large filamentous protein (single peptide) with a molecular mass of approximately 3 MDa, contour length approximately 900 nm, and diameter approximately 4 nm, and resides in striated muscle. Connectin links the thick filaments to the Z-lines in a sarcomere and produces a passive elastic force when muscle fiber is stretched. The aim of this study is to elucidate some aspects of physical properties of isolated beta-connectin (titin 2), a proteolytic fragment of connectin, by means of dynamic light-scattering (DLS) spectroscopy. The analysis of DLS spectra for beta-connectin gave the translational diffusion coefficient of 3.60 x 10(-8) cm2/s at 10 degrees C (or the hydrodynamic radius of 44.1 nm), molecular mass little smaller than 3.0 MDa (for a literature value of sedimentation coefficient), the root-mean-square end-to-end distance of 163 nm (or the radius of gyration of 66.6 nm), and the Kuhn segment number of 30 and segment length of 30 nm (or the persistence length of 15 nm). These results permitted to estimate the flexural rigidity of 6.0 x 10(-20) dyn x cm2 for filament bending, and the elastic constant of 7 dyn/cm for extension of one persistence length. Based on a simple model, implications of the present results in muscle physiology are discussed.

journal_name

Biophys J

journal_title

Biophysical journal

authors

Higuchi H,Nakauchi Y,Maruyama K,Fujime S

doi

10.1016/S0006-3495(93)81261-X

subject

Has Abstract

pub_date

1993-11-01 00:00:00

pages

1906-15

issue

5

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(93)81261-X

journal_volume

65

pub_type

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