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Related Concept Videos

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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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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

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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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Measuring Transcellular Interactions through Protein Aggregation in a Heterologous Cell System
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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)
|November 13, 2023
PubMed
Summary
This summary is machine-generated.

Controlling protein aggregation at interfaces is key for understanding biological functions and advancing biopolymer materials. This review details interface-mediated assembly strategies for nanoscale to macroscale biopolymer structures.

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Area of Science:

  • Biopolymer Science
  • Materials Science
  • Surface Chemistry

Background:

  • Protein aggregation at interfaces plays critical roles in physiological processes and can lead to dysfunction.
  • Understanding interfacial effects on biopolymer assembly is vital for both biological function and material applications.
  • Rational design of interactions between building blocks and interfaces enables control over complex biopolymer structures.

Purpose of the Study:

  • To review recent advancements in interface-mediated assembly and properties of biopolymer materials.
  • To highlight strategies for controlling biopolymer assembly across various scales (nano- to macroscale).
  • To stimulate integration and progression in the science of interfacial assembled biopolymer materials.

Main Methods:

  • Review of solid-liquid interface (SIL)-mediated biopolymer assembly, including inorganic templates and phase transitions.
  • Discussion of air-water interface (AWI)-instigated biopolymer assembly, emphasizing its role in energy conversion.
  • Summary of liquid-liquid interface (LLI)-mediated biopolymer assembly and associated applications.

Main Results:

  • Progress in controlling interfacial assembly structures of biopolymers from nanoscale to macroscale.
  • Demonstration of diverse interface types (SIL, AWI, LLI) driving specific biopolymer assembly mechanisms.
  • Identification of potential for advanced applications through rational design of interfacial biopolymer materials.

Conclusions:

  • Interface-mediated assembly offers powerful strategies for developing advanced biopolymer materials.
  • Further research into interfacial phenomena will drive innovation in biopolymer science and applications.
  • This review provides a foundation for future advancements in the field of interfacial assembled biopolymers.