Unfolding of Titin Domains Explains the Viscoelastic Behavior of Skeletal Myofibrils
Author:
Publisher
Elsevier BV
Subject
Biophysics
Reference44 articles.
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2. Evidence that the tandem Ig domains near the end of the muscle thick filament form an inelastic part of the I-band titin;Bennett;J. Struct. Biol.,1997
3. Evidence for cross-bridge attachment in relaxed muscle at low ionic strength;Brenner;Proc. Natl. Acad. Sci. U.S.A.,1982
4. Mechanical and chemical unfolding of a single protein: a comparison;Carrion-Vazquez;Proc. Natl. Acad. Sci. U.S.A.,1999
5. Reversible unfolding of fibronectin type III and immunoglobulin domains provides the structural basis for stretch and elasticity of titin and fibronectin;Erickson;Proc. Natl. Acad. Sci. U.S.A.,1994
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