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Related Concept Videos

Protein Denaturation01:28

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The function of proteins depends on their native three-dimensional structure, which is dictated by the amino acid sequence of the specific protein. Folding of the polypeptide chain takes place under specific conditions that energetically favor the folded conformation. In contrast, protein denaturation occurs spontaneously under unfavorable conditions that disrupt the integrity of the folded conformation. Thus, the chemical and physical environment of a protein, such as significant changes in pH...
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The Proteasome01:13

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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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Within a biological system, the DNA encodes the RNA, and the nucleotide sequence in the RNA further defines the amino acid sequence in the protein. This is referred to as “The Central Dogma of Molecular Biology” - a term coined by Francis Crick.  Central dogma is a firm principle in biology that defines the flow of genetic information within any life form. The two fundamental steps in central dogma are - transcription and translation.
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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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Related Experiment Video

Updated: Feb 17, 2026

Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans
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Environment-transformable sequence-structure relationship: a general mechanism for proteotoxicity.

Jianxing Song1

  • 1Department of Biological Sciences, Faculty of Science, National University of Singapore, 10 Kent Ridge Crescent, Singapore, 119260, Singapore. dbssjx@nus.edu.sg.

Biophysical Reviews
|December 6, 2017
PubMed
Summary

Proteins can change their structure and interact with membranes, potentially causing disease and aging. This environment-driven transformation offers a new view on protein toxicity.

Keywords:
AgingLiquid–liquid phase separation (LLPS)Membrane interactionNeurodegenerative diseasesPrion-like domainsProteotoxicity

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Proteins are classified as membrane or non-membrane, but their interconversion is unknown.
  • Aging and diseases convert well-folded proteins into toxic, insoluble forms via unclear mechanisms.
  • The "Salting-in" dogma traditionally explains protein solubility.

Purpose of the Study:

  • To investigate the "insoluble" protein regime beyond the "Salting-in" dogma.
  • To explore the mechanisms behind the conversion of proteins into toxic, "insoluble" forms.
  • To understand the role of protein-environment interactions in disease and aging.

Main Methods:

  • Solubilization of "insoluble" proteins, including integral membrane fragments, in ion-minimized water.
  • Study of "insoluble" forms of specific proteins: P56S-MSP, L126Z-SOD1, nascent SOD1, C71G-Profilin1, and E. coli S1 fragments.
  • Analysis of protein structures and their interactions with aqueous and membrane environments.

Main Results:

  • "Insoluble" proteins were found to be unfolded or co-existing with unfolded states.
  • Unfolded protein states demonstrated a novel capacity for membrane interaction, driven by helix/loop formation.
  • Proteins possess segments capable of adopting distinct structures in aqueous and membrane environments.
  • Abnormal membrane interactions may initiate disease and aging processes.

Conclusions:

  • Proteins can transform between aqueous and membrane-compatible structures based on their environment.
  • This environment-transformable sequence-structure relationship may be a general mechanism for proteotoxicity.
  • Abnormal protein-membrane interactions, coupled with aggregation, can lead to severe proteotoxicity and damaged organelles.