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Related Concept Videos

Protein-protein Interfaces02:04

Protein-protein Interfaces

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Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
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Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
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Protein Complex Assembly02:41

Protein Complex Assembly

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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.
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Molecular Chaperones and Protein Folding03:00

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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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Protein Networks02:26

Protein Networks

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An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
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Cooperative Allosteric Transitions01:58

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Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
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Updated: Jul 9, 2025

Measuring Transcellular Interactions through Protein Aggregation in a Heterologous Cell System
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Measuring Transcellular Interactions through Protein Aggregation in a Heterologous Cell System

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Correction: Interface-mediated protein aggregation.

Fei Tao1, Qian Han1, Peng Yang1

  • 1Key laboratory of Applied Surface and Colloid Chemistry, Ministry of Education, School of Chemistry and Chemical Engineering, Shaanxi Normal University, Xi'an 710119, China. yangpeng@snnu.edu.cn.

Chemical Communications (Cambridge, England)
|December 5, 2023
PubMed
Summary
This summary is machine-generated.

This correction clarifies findings on interface-mediated protein aggregation. It ensures accurate understanding of how surfaces influence protein behavior and potential aggregation pathways.

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Area of Science:

  • Biochemistry
  • Materials Science
  • Chemical Engineering

Context:

  • Protein aggregation is implicated in various diseases and material degradation.
  • Understanding the role of interfaces is crucial for controlling protein behavior.
  • Previous research explored interface-mediated protein aggregation.

Purpose:

  • To correct specific details in the original publication 'Interface-mediated protein aggregation'.
  • To ensure the accuracy of data and interpretations regarding protein-surface interactions.
  • To provide a corrected reference for future studies in the field.

Summary:

  • The correction addresses errors in the original article concerning the mechanisms of protein aggregation at interfaces.
  • Specific experimental data or analytical interpretations have been revised for greater precision.
  • The corrected information pertains to the influence of surface properties on protein conformational changes and subsequent aggregation.

Impact:

  • Ensures the scientific record is accurate for researchers studying protein aggregation.
  • Facilitates reliable development of strategies to prevent or utilize protein aggregation.
  • Supports advancements in areas like biomaterials, drug delivery, and diagnostics.