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Related Concept Videos

The Proteasome01:13

The Proteasome

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Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
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The Proteasome02:18

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Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
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Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

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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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The Proteasome Structure01:17

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The ubiquitin-proteasome pathway is a well-known mechanism utilized by eukaryotic cells to remove cytoplasmic proteins that are misfolded, damaged, or no longer needed. In this pathway, the protein that needs to be eliminated undergoes a process called ubiquitination, where a chain of ubiquitin molecules is attached to the 48th lysine residue of the target protein. This ubiquitin modification helps the proteasome distinguish between a target protein and a healthy protein.
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Regulated Protein Degradation02:58

Regulated Protein Degradation

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It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
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Protein Modifications in the RER01:26

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Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
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Purification of Hsp104, a Protein Disaggregase
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Purification of Hsp104, a Protein Disaggregase

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Surface-mediated protein disaggregation.

Mithun Radhakrishna1, Sanat K Kumar

  • 1Department of Chemical Engineering, Columbia University , New York, New York 10027, United States.

Langmuir : the ACS Journal of Surfaces and Colloids
|March 5, 2014
PubMed
Summary
This summary is machine-generated.

Preventing protein aggregation involves tuning surface properties. Increasing surface hydrophobicity reduces protein-protein interactions, while optimal pore sizes enhance this effect through confinement.

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Area of Science:

  • Biophysics
  • Materials Science
  • Protein Chemistry

Background:

  • Protein aggregation is a significant challenge in biological systems and industrial applications.
  • Hydrophobic interactions between protein residues are the primary drivers of aggregation.
  • Controlling protein-protein interactions is crucial for preventing aggregation.

Purpose of the Study:

  • To investigate how surface chemistry and curvature influence interprotein interactions.
  • To identify optimal surface properties for mitigating protein aggregation.
  • To explore the role of confinement in protein stabilization.

Main Methods:

  • Utilized the Hydrophobic-Polar (HP) lattice model for calculations.
  • Simulated protein adsorption on surfaces with varying hydrophobicity and curvature.
  • Analyzed interprotein contacts, surface contacts, and native contacts.

Main Results:

  • Interprotein interactions significantly decrease upon increasing surface hydrophobicity to a critical adsorption transition point.
  • At this critical hydrophobicity, proteins favor surface contacts over interprotein contacts.
  • Adsorption within hydrophobic pores of optimal size is highly effective in reducing aggregation while preserving native structure.

Conclusions:

  • Surface hydrophobicity can be engineered to effectively prevent protein aggregation.
  • Confinement within optimally sized hydrophobic pores offers a dual benefit of reducing aggregation and stabilizing native protein conformations.
  • These findings provide insights for designing surfaces and materials to control protein behavior.