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Post-translational Translocation of Proteins to the RER01:27

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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.
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After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...
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During the electron transport chain, electrons from NADH and FADH2 are first transferred to complexes I and II, respectively. These two complexes then transfer the electrons to ubiquinol, which carries them further to complex III. Complex III passes the electrons across the intermembrane space to Cyt c, which carries them further to complex IV. Complex IV donates electrons to oxygen and reduces it to water. As electrons pass through complexes I, III, and IV, the energy released aids the pumping...
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After budding out from the ER membrane, some COPII vesicles lose their coat and fuse with one another to form larger vesicles and interconnected tubules called vesicular tubular clusters or VTCs. These clusters constitute a compartment at the ER-Golgi interface known as ERGIC (Endoplasmic Reticulum Golgi Intermediate Compartment). The ERGIC is a mobile membrane-bound cargo transport system that sorts proteins secreted from ER and delivers them to the Golgi.
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The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
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Updated: Dec 11, 2025

Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy
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Unfolding cytochromes c-b562 and Rd apo b562.

John J Kozak1, Harry B Gray2, Roberto A Garza-López3

  • 1Department of Chemistry, DePaul University, Chicago, IL 60604-6116, United States of America.

Journal of Inorganic Biochemistry
|August 21, 2020
PubMed
Summary
This summary is machine-generated.

We analyzed protein unfolding in cytochromes c-b562 and apo b562, revealing distinct helix unfolding orders. The interior helix of cytochrome c-b562 folds first, potentially protecting the heme group.

Keywords:
AngularApoproteinCytochromesHoloproteinMisligationUnfolding

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Area of Science:

  • Structural biology
  • Protein dynamics
  • Biophysics

Background:

  • Cytochromes c-b562 and apo b562 are crucial proteins with distinct structures.
  • Understanding protein unfolding is key to comprehending protein function and misfolding diseases.

Purpose of the Study:

  • To analyze and compare the early stages of unfolding in cytochromes c-b562 and apo b562.
  • To identify differences in helix unfolding order between the two proteins based on structural analysis.

Main Methods:

  • Geometrical analysis of crystal structures (PDB IDs: 2BC5, 1YYJ).
  • Quantification of spatial and angular changes during denaturation, residue-by-residue.
  • Two independent analyses: spatial metrics and angular metrics.

Main Results:

  • Established distinct helix unfolding orders for both proteins.
  • Identified differential unfolding patterns for N-terminal and C-terminal helices.
  • Quantified excluded-volume effects and volume changes during unfolding.

Conclusions:

  • The interior helix of cytochrome c-b562 is the first to fold, suggesting a role in heme protection.
  • Protein unfolding pathways are influenced by sequence differences and structural features.
  • Findings support a model of ultrafast protein folding via a minimally frustrated landscape.