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Related Concept Videos

Viral Structure00:56

Viral Structure

Viruses are extraordinarily diverse in shape and size, but they all have several structural features in common. All viruses have a core that contains a DNA- or RNA-based genome. The core is surrounded by a protective coat of proteins called the capsid. The capsid is composed of subunits called capsomeres. The capsid and genome-containing core are together known as the nucleocapsid.
Introduction to Virus01:28

Introduction to Virus

Viruses are unique biological entities that blur the boundary between living and non-living systems. Although they lack cellular structure and metabolic processes, they can exhibit characteristics of life when infecting a host. Their defining feature is a nucleic acid core, composed of either DNA or RNA, encapsulated within a protein coat called a capsid. This simple structure allows them to invade host cells and use their machinery for replication efficiently.Viral Structure and...
Size and Structure of Viral Genomes01:26

Size and Structure of Viral Genomes

Viral genomes exhibit remarkable diversity in size, structure, and composition, influencing their replication strategies and interactions with host cells. These genomes consist of either DNA or RNA and may be linear or circular. Additionally, they can be single-stranded or double-stranded, with each configuration affecting how the virus propagates within a host. RNA viruses, for instance, generally have smaller genomes than DNA viruses, a factor that contributes to their high mutation rates and...
Viruses with RNA Genomes01:29

Viruses with RNA Genomes

RNA viruses are categorized into positive-strand, negative-strand, or double-stranded groups based on their genomic structure and replication mechanisms. This classification dictates how they exploit host cellular machinery for protein synthesis and replication. Some RNA viruses also utilize reverse transcription as part of their life cycle, further diversifying their replication strategies.Positive-Strand RNA VirusesPositive-strand RNA viruses have genomes that function directly as messenger...
Leaky Scanning02:28

Leaky Scanning

During most eukaryotic translation processes, the small 40S ribosome subunit scans an mRNA from its 5' end until it encounters the first start AUG codon. The large 60S ribosomal subunit then joins the smaller one to initiate protein synthesis. The location of the translation initiation is largely determined by the nucleotides near the start codon as there may be multiple translation initiation sites present on the mRNA.  Marilyn Kozak discovered that the sequence RCCAUGG (where R stands for...
Viruses of Archaea01:29

Viruses of Archaea

Archaeal viruses play a crucial role in the ecosystems of extremophilic archaea, particularly those belonging to the phyla Euryarchaeota and Crenarchaeota. By shaping host evolution and facilitating gene transfer, these viruses influence microbial communities and contribute to genetic diversity in extreme environments. The archaea they infect thrive in acidic hot springs and hydrothermal vents characterized by high temperatures and low pH. Archaeal viruses exhibit remarkable structural...

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Profiling of Surface Protein Epitopes on Viral Particles by Multiplex Dual-Reporter Strategy
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Profiling of Surface Protein Epitopes on Viral Particles by Multiplex Dual-Reporter Strategy

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Do viral proteins possess unique biophysical features?

Nobuhiko Tokuriki1, Christopher J Oldfield, Vladimir N Uversky

  • 1Department of Biological Chemistry, Weizmann Institute of Science, Rehovot 76100, Israel.

Trends in Biochemical Sciences
|December 9, 2008
PubMed
Summary

Highly thermostable proteins are compact, while viral proteins often have disordered segments. This structural difference may reflect distinct adaptation strategies in different environments.

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Flow Virometry to Analyze Antigenic Spectra of Virions and Extracellular Vesicles

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Area of Science:

  • Biophysics
  • Molecular Biology
  • Evolutionary Biology

Background:

  • Natural selection optimizes protein sequence, structure, and biophysical properties for specific environments.
  • Highly thermostable proteins exhibit compact structures with packed hydrophobic cores and charged surfaces.
  • Viral proteins, particularly RNA viral proteins, often feature disordered segments and less-packed cores.

Purpose of the Study:

  • To investigate the hypothesis that highly thermostable proteins and viral proteins represent opposing adaptation strategies.
  • To explore the structural and functional implications of protein adaptations in different biological contexts.

Main Methods:

  • Comparative analysis of protein structural features.
  • Examination of biophysical properties of thermostable and viral proteins.
  • Correlation of structural characteristics with environmental adaptation and viral function.

Main Results:

  • Thermostable proteins are characterized by high compactness, well-packed hydrophobic cores, and charged surfaces.
  • Viral proteins, especially RNA viral proteins, show a higher prevalence of disordered segments and loosely packed cores.
  • These viral protein features may enhance structural flexibility and host interaction, potentially buffering mutation effects.

Conclusions:

  • Protein structural properties are finely tuned by natural selection for environmental adaptation.
  • Thermostable and viral proteins exemplify contrasting adaptation strategies, with implications for protein function and evolution.
  • The structural flexibility of viral proteins could be crucial for their adaptability and interaction with host systems.