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Related Concept Videos

Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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.
The...
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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.
The...
Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

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 translocon complex.
The Proteasome Structure01:17

The Proteasome Structure

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.
The proteasome is an...

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Chaperonin structure: the large multi-subunit protein complex.

Mateusz Banach1,2, Katarzyna Stąpor2,3, Irena Roterman1,2

  • 1Department of Bioinformatics and Telemedicine - Jagiellonian University, Collegium Medicum, Lazarza 16, 31-531 Krakow, Poland.

International Journal of Molecular Sciences
|April 29, 2009
PubMed
Summary
This summary is machine-generated.

Chaperonins like GroEL and GroES use ATP to aid protein folding. Analyzing hydrophobicity reveals how their structure, with hydrophobic cores and hydrophilic surfaces, dictates their function in protein folding.

Keywords:
Protein foldingchaperoninhydrophobicity

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Area of Science:

  • Structural biology
  • Biochemistry
  • Molecular biology

Background:

  • Chaperonins are essential multi-subunit protein complexes that facilitate protein folding.
  • These proteins require ATP to assist in the proper folding of other proteins.
  • The GroEL-GroES system is a well-studied example of a chaperonin.

Purpose of the Study:

  • To analyze the hydrophobicity distribution in chaperonin structures (GroEL and GroES).
  • To investigate the relationship between the structure and function of chaperonins.
  • To explore how hydrophobicity influences protein folding assistance.

Main Methods:

  • Analysis of hydrophobicity distribution in GroEL and GroES polypeptide chains.
  • Comparison of empirical residue distribution with a theoretical model of hydrophobic cores and hydrophilic surfaces.
  • Generation of a hydrophobic force field structure for the chaperonin capsule.

Main Results:

  • A discrepancy was observed between the empirical and theoretical hydrophobicity distributions.
  • This discrepancy appears to be functionally significant, linking structure to chaperonin activity.
  • A specific hydrophobic force field generated by the chaperonin capsule was elucidated.

Conclusions:

  • The specific arrangement of hydrophobic and hydrophilic residues in chaperonins is crucial for their function.
  • The identified hydrophobic force field likely plays a role in substrate protein folding.
  • Further investigation into this force field could reveal detailed mechanisms of chaperonin-assisted folding.