Probing the Mechanical Folding Kinetics of TAR RNA by Hopping, Force-Jump, and Force-Ramp Methods

نویسندگان
چکیده

برای دانلود رایگان متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Probing the mechanical folding kinetics of TAR RNA by hopping, force-jump, and force-ramp methods.

Mechanical unfolding and refolding of single RNA molecules have previously been observed in optical traps as sudden changes in molecular extension. Two methods have been traditionally used: "force-ramp", with the applied force continuously changing, and "hopping". In hopping experiments the force is held constant and the molecule jumps spontaneously between two different states. Unfolding/refol...

متن کامل

Probing complex RNA structures by mechanical force.

RNA secondary structures of increasing complexity are probed combining single molecule stretching experiments and stochastic unfolding/refolding simulations. We find that force-induced unfolding pathways cannot usually be interpreted by solely invoking successive openings of native helices. Indeed, typical force-extension responses of complex RNA molecules are largely shaped by stretching-induc...

متن کامل

Determination of thermodynamics and kinetics of RNA reactions by force.

Single-molecule methods have made it possible to apply force to an individual RNA molecule. Two beads are attached to the RNA; one is on a micropipette, the other is in a laser trap. The force on the RNA and the distance between the beads are measured. Force can change the equilibrium and the rate of any reaction in which the product has a different extension from the reactant. This review desc...

متن کامل

The unfolding and folding dynamics of TNfnALL probed by single molecule force–ramp spectroscopy

Tenascin, an important extracellular matrix protein, is subject to stretching force under physiological conditions and plays important roles in regulating the cell–matrix interactions. Using the recently developed single molecule force–ramp spectroscopy, we investigated the unfolding– folding kinetics of a recombinant tenascin fragment TNfnALL. Our results showed that all the 15 FnIII domains i...

متن کامل

The force-dependent mechanism of DnaK-mediated mechanical folding

It is well established that chaperones modulate the protein folding free-energy landscape. However, the molecular determinants underlying chaperone-mediated mechanical folding remain largely elusive, primarily because the force-extended unfolded conformation fundamentally differs from that characterized in biochemistry experiments. We use single-molecule force-clamp spectroscopy, combined with ...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

ژورنال

عنوان ژورنال: Biophysical Journal

سال: 2006

ISSN: 0006-3495

DOI: 10.1529/biophysj.105.068049