Mechanism of Titin Unfolding by Force: Insight from Quasi-Equilibrium Molecular Dynamics Calculations
نویسندگان
چکیده
منابع مشابه
Unfolding of titin immunoglobulin domains by steered molecular dynamics simulation.
Titin, a 1-microm-long protein found in striated muscle myofibrils, possesses unique elastic and extensibility properties in its I-band region, which is largely composed of a PEVK region (70% proline, glutamic acid, valine, and lysine residue) and seven-strand beta-sandwich immunoglobulin-like (Ig) domains. The behavior of titin as a multistage entropic spring has been shown in atomic force mic...
متن کاملSteered molecular dynamics studies of titin I1 domain unfolding.
The cardiac muscle protein titin, responsible for developing passive elasticity and extensibility of muscle, possesses about 40 immunoglobulin-like (Ig) domains in its I-band region. Atomic force microscopy (AFM) and steered molecular dynamics (SMD) have been successfully combined to investigate the reversible unfolding of individual Ig domains. However, previous SMD studies of titin I-band mod...
متن کاملStepwise unfolding of titin under force-clamp atomic force microscopy.
Here we demonstrate the implementation of a single-molecule force clamp adapted for use with an atomic force microscope. We show that under force-clamp conditions, an engineered titin protein elongates in steps because of the unfolding of its modules and that the waiting times to unfold are exponentially distributed. Force-clamp measurements directly measure the force dependence of the unfoldin...
متن کاملDynamics of equilibrium folding and unfolding transitions of titin immunoglobulin domain under constant forces.
The mechanical stability of force-bearing proteins is crucial for their functions. However, slow transition rates of complex protein domains have made it challenging to investigate their equilibrium force-dependent structural transitions. Using ultra stable magnetic tweezers, we report the first equilibrium single-molecule force manipulation study of the classic titin I27 immunoglobulin domain....
متن کاملComputer modeling of force-induced titin domain unfolding.
Titin, a 1 micron long protein found in striated muscle myofibrils, possesses unique elastic and extensibility properties, and is largely composed of a PEVK region and beta-sandwich immunoglobulin (Ig) and fibronectin type III (FnIII) domains. The extensibility behavior of titin has been shown in atomic force microscope and optical tweezer experiments to partially depend on the reversible unfol...
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ژورنال
عنوان ژورنال: Biophysical Journal
سال: 2006
ISSN: 0006-3495
DOI: 10.1529/biophysj.106.082594