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Related Concept Videos

Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

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Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
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Energy to Drive Translocation01:37

Energy to Drive Translocation

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Mitochondrial protein import is powered by two distinct energy sources: ATP hydrolysis and electrochemical potential across the inner membrane. Newly synthesized precursors are bound by cytosolic chaperones of the Hsp70 family, which guide them to the import receptors on the mitochondrial surface. Utilizing the energy of ATP hydrolysis, Hsp70 chaperones transfer these precursors to the TOM receptors on the mitochondrial outer membrane.
Generally, polypeptides are unfolded by two distinct...
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Cotranslational Protein Translocation01:20

Cotranslational Protein Translocation

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Translocation of proteins across membranes is an ancient process that occurs even in bacteria and archaebacteria. In fact, the components of the translocation machinery are still conserved between prokaryotes and eukaryotes.
Sec61 channel partners for cotranslational translocation
During cotranslational translocation, the Sec61 channel partners with the signal recognition particle (SRP), the signal recognition particle receptor (SR), and the ribosomes to transport the nascent polypeptide chain...
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Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

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The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the...
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Bacterial Translocation and Protein Secretion01:26

Bacterial Translocation and Protein Secretion

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Bacterial protein secretion involves translocation systems to ensure proteins reach their designated locations, including the plasma membrane, periplasm, outer membrane, or the external environment. These translocation systems are vital for bacterial physiology, supporting processes like membrane assembly, enzymatic activity in the periplasm, and interactions with the external environment. The division of labor between Sec and Tat pathways ensures efficiency in handling proteins with diverse...
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Post-translational Translocation of Proteins to the RER01:27

Post-translational Translocation of Proteins to the RER

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A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
Targeting proteins to the ER
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Determination of Zeta Potential via Nanoparticle Translocation Velocities through a Tunable Nanopore: Using DNA-modified Particles as an Example
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Translocation of Star Polyelectrolytes through a Nanopore.

Karthik Nagarajan1, Shing Bor Chen1

  • 1Department of Chemical & Biomolecular Engineering , National University of Singapore , 117585 , Singapore.

The Journal of Physical Chemistry. B
|March 20, 2019
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Electric field driven translocation of charged star polymers through nanopores is feasible. Critical field strength and translocation time depend on polymer architecture, enabling potential separation of different star polyelectrolytes.

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Area of Science:

  • Polymer Physics
  • Nanotechnology
  • Computational Chemistry

Background:

  • Charged polymers are crucial in nanotechnology and biological systems.
  • Understanding polymer behavior in confined geometries like nanopores is essential for developing advanced materials and separation techniques.
  • Electric field driven translocation offers a potential method for manipulating and separating polymers at the nanoscale.

Purpose of the Study:

  • To investigate the electric field driven translocation of charged star polymers through a cylindrical nanopore.
  • To determine the influence of star polymer architecture (number of arms, beads per arm) on translocation dynamics.
  • To explore the feasibility of using this method for separating star polyelectrolytes.

Main Methods:

  • Dissipative particle dynamics (DPD) simulations were employed to model the translocation process.
  • Systematic variation of star polymer parameters (number of arms, beads per arm) was performed.
  • Analysis of critical field strength, translocation time, and polymer conformation within the nanopore.

Main Results:

  • The critical electric field strength for translocation is dependent on the number of arms and beads per arm.
  • Average translocation time shows a nonmonotonic relationship with the number of arms under good solvent conditions.
  • Star polymers with more arms experience less stretching along the pore axis compared to linear polymers.
  • Tension in star polymers localizes near the branch point, influencing translocation dynamics differently than linear chains.

Conclusions:

  • Electric field driven translocation is a viable method for moving charged star polymers through nanopores.
  • The distinct dependence of translocation dynamics on star polymer architecture suggests potential for size-based or structural separation of polyelectrolytes.
  • The unique tension distribution in star polymers presents specific challenges and characteristics during nanopore passage.