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Related Concept Videos

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Intrinsically Disordered Proteins

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Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
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Simple proteins and protein complexes contain only amino acids. In contrast, many other proteins, called conjugated proteins, covalently bond with non-protein moieties.
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Protein Complex Assembly02:41

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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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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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Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
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Related Experiment Video

Updated: Jul 10, 2025

Production of a SARS-CoV-2 Virus-Like-Particle System to Investigate Viral Life Cycles In Vitro
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Production of a SARS-CoV-2 Virus-Like-Particle System to Investigate Viral Life Cycles In Vitro

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Intrinsically disordered proteins and liquid-liquid phase separation in SARS-CoV-2 interactomes.

Lazar M Vasović1, Gordana M Pavlović-Lažetić1, Jovana J Kovačević1

  • 1Faculty of Mathematics, University of Belgrade, Belgrade, Serbia.

Journal of Cellular Biochemistry
|November 22, 2023
PubMed
Summary

This study analyzed SARS-CoV-2 proteins, finding that highly connected viral proteins are more ordered, unlike in eukaryotic systems. This challenges previous research on viral interactomes and protein disorder.

Keywords:
SARS‐CoV‐2correlation analysisinteractomicsintrinsically disordered proteins (IDPs)intrinsically disordered regions (IDRs)liquid–liquid phase separation (LLPS)viral–host interactomes

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Area of Science:

  • Virology
  • Computational Biology
  • Structural Biology

Background:

  • Proteins play crucial roles in viral functions and host interactions.
  • Understanding the structural properties of viral proteins, like disorder and connectivity, is key to deciphering viral mechanisms.
  • The SARS-CoV-2 proteome's interactome properties, including protein disorder, are not fully understood.

Purpose of the Study:

  • To investigate the relationship between protein disorder, connectivity, and phase separation in SARS-CoV-2 interactomes.
  • To explore potential links between viral protein disorder and host-viral interactions within the human lung interactome.
  • To compare the properties of viral protein interaction networks with those of eukaryotic systems.

Main Methods:

  • Analysis of SARS-CoV-2 proteome subsets (membrane, nonstructural, full proteome).
  • Evaluation of protein disorder, liquid-liquid phase separation (LLPS) probabilities, and node degrees in interaction networks.
  • Integration of viral interactomes with human lung tissue interactome for host-viral interaction analysis.
  • Correlation analysis to assess relationships between protein features and network properties.

Main Results:

  • No clear correlation found between raw protein disorder and other features.
  • A positive correlation observed between protein disorder and the mean disorder of its neighbors.
  • Highly connected viral proteins (hubs) showed a tendency towards being more ordered compared to less connected proteins.
  • Viral-host interactome analysis suggested potential links between new connections and protein disorder.

Conclusions:

  • Viral protein interaction networks exhibit distinct properties compared to eukaryotic interactomes, particularly regarding protein disorder and hub connectivity.
  • The findings suggest that viral hubs may be more structurally ordered, contrasting with previous observations in eukaryotic systems.
  • Further research is warranted to explore these unique characteristics and their implications for viral pathogenesis and therapeutic strategies.