Prion Protein Translocation Mechanism Revealed by Pulling Force Studies

نویسندگان
چکیده

برای دانلود باید عضویت طلایی داشته باشید

برای دانلود 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

Protein translocation: Is Hsp70 pulling my chain?

Hsp70 proteins in the lumen of the endoplasmic reticulum and in the mitochondrial matrix are thought to drive the translocation of proteins into each organelle. Recent experiments aimed at distinguishing between two models for Hsp70 function appear to reach opposite conclusions.

متن کامل

Polymer translocation through a nanopore under a pulling force.

We investigate polymer translocation through a nanopore under a pulling force using Langevin dynamics simulations. We concentrate on the influence of the chain length N and the pulling force F on the translocation time tau . The distribution of tau is symmetric and narrow for strong F . We find that tau approximately N{2} and translocation velocity v approximately N{-1} for both moderate and st...

متن کامل

Protein High-Force Pulling Simulations Yield Low-Force Results

All-atom explicit-solvent molecular dynamics simulations are used to pull with extremely large constant force (750-3000 pN) on three small proteins. The introduction of a nondimensional timescale permits direct comparison of unfolding across all forces. A crossover force of approximately 1100 pN divides unfolding dynamics into two regimes. At higher forces, residues sequentially unfold from the...

متن کامل

Hsp70 chaperones accelerate protein translocation and the unfolding of stable protein aggregates by entropic pulling.

Hsp70s are highly conserved ATPase molecular chaperones mediating the correct folding of de novo synthesized proteins, the translocation of proteins across membranes, the disassembly of some native protein oligomers, and the active unfolding and disassembly of stress-induced protein aggregates. Here, we bring thermodynamic arguments and biochemical evidences for a unifying mechanism named entro...

متن کامل

Mechanism of trans-translation revealed by in vitro studies

tmRNA is a bacterial small RNA having a structure resembling the upper half of tRNA and its 3' end accepts alanine followed by binding to EF-Tu like tRNA. Instead of lacking a lower half of the cloverleaf structure including the anticodon, tmRNA has a short coding sequence for tag-peptide that serves as a target of cellular proteases. An elaborate coordination of two functions as tRNA and mRNA ...

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: Journal of Molecular Biology

سال: 2020

ISSN: 0022-2836

DOI: 10.1016/j.jmb.2020.05.022