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Related Concept Videos

Riboswitches01:56

Riboswitches

Riboswitches are non-coding mRNA domains that regulate the transcription and translation of downstream genes without the help of proteins. Riboswitches bind directly to a metabolite and can form unique stem-loop or hairpin structures in response to the amount of the metabolite present. They have two distinct regions – a metabolite-binding aptamer and an expression platform.
The aptamer has high specificity for a particular metabolite which allows riboswitches to specifically regulate...
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Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
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Energy to Drive Translocation01:37

Energy to Drive Translocation

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...
Mitochondrial Precursor Proteins01:39

Mitochondrial Precursor Proteins

Mitochondrial precursors are partially unfolded or loosely folded polypeptide chains. Newly synthesized precursors are inhibited from spontaneously folding into their native conformation by the cytosolic chaperones, heat shock proteins 70 (Hsp70), and mitochondrial import stimulation factors (MSFs). Precursors bound to MSFs are guided to the TOM70-TOM37 receptors, while precursors bound to Hsp70  chaperones are targetted to TOM20-TOM22 receptor complexes.
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Subviral Agents01:29

Subviral Agents

Subviral agents are infectious entities that resemble viruses but lack one or more viral components, such as a capsid or essential replication machinery. These agents include viroids, prions, and satellites, each possessing distinct structural and functional characteristics that influence their mode of infection and replication.Viroids are the simplest subviral agents, consisting of circular, single-stranded RNA molecules without a protein coat. They exclusively infect plants, relying entirely...

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Related Experiment Video

Updated: May 30, 2026

Purification and Refolding to Amyloid Fibrils of (His)6-tagged Recombinant Shadoo Protein Expressed as Inclusion Bodies in E. coli
09:43

Purification and Refolding to Amyloid Fibrils of (His)6-tagged Recombinant Shadoo Protein Expressed as Inclusion Bodies in E. coli

Published on: December 19, 2015

The prion protein binds thiamine.

Rolando Perez-Pineiro1, Trent C Bjorndahl, Mark V Berjanskii

  • 1Department of Biological Sciences, University of Alberta, Edmonton, AB, Canada.

The FEBS Journal
|August 19, 2011
PubMed
Summary
This summary is machine-generated.

Researchers identified thiamine (vitamin B1) as a specific ligand for the prion protein. This interaction is evolutionarily conserved and involves vitamin B1 binding to the prion protein, offering insights into its biological function.

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Last Updated: May 30, 2026

Purification and Refolding to Amyloid Fibrils of (His)6-tagged Recombinant Shadoo Protein Expressed as Inclusion Bodies in E. coli
09:43

Purification and Refolding to Amyloid Fibrils of (His)6-tagged Recombinant Shadoo Protein Expressed as Inclusion Bodies in E. coli

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Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans
12:57

Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans

Published on: January 8, 2015

Area of Science:

  • Biochemistry
  • Neuroscience
  • Molecular Biology

Background:

  • The prion protein (PrP) is highly conserved, but its precise biological role remains elusive.
  • Understanding PrP function is crucial for neurodegenerative disease research.

Purpose of the Study:

  • To identify potential biological functions of the prion protein through small-molecule screening.
  • To investigate the interaction between the prion protein and water-soluble metabolites.

Main Methods:

  • Conducted a small-molecule screening assay using Syrian hamster prion protein [shPrP(90-232)].
  • Utilized 1D NMR, fluorescence quenching, and surface plasmon resonance to identify ligands.
  • Employed heteronuclear NMR, docking, and molecular dynamics to characterize the binding site and interactions.

Main Results:

  • Identified thiamine (vitamin B1) as a specific prion protein ligand with a binding constant of ~60 μM.
  • Demonstrated evolutionary conservation of thiamine-prion protein interaction across mouse, hamster, and human PrP.
  • Found that thiamine monophosphate and thiamine diphosphate also bind the prion protein with similar affinity.
  • Localized the thiamine-binding site to the region between helix 1 and the preceding loop.

Conclusions:

  • Thiamine is a specific, evolutionarily conserved ligand for the prion protein.
  • The N-terminus of the prion protein does not influence thiamine binding.
  • The study provides a model for the thiamine-binding pharmacophore and its interaction site on the prion protein.