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Related Concept Videos

Metallic Solids02:37

Metallic Solids

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Metallic solids such as crystals of copper, aluminum, and iron are formed by metal atoms. The structure of metallic crystals is often described as a uniform distribution of atomic nuclei within a “sea” of delocalized electrons. The atoms within such a metallic solid are held together by a unique force known as metallic bonding that gives rise to many useful and varied bulk properties.
All metallic solids exhibit high thermal and electrical conductivity, metallic luster, and malleability....
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Structures of Solids02:22

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Solids in which the atoms, ions, or molecules are arranged in a definite repeating pattern are known as crystalline solids. Metals and ionic compounds typically form ordered, crystalline solids. A crystalline solid has a precise melting temperature because each atom or molecule of the same type is held in place with the same forces or energy. Amorphous solids or non-crystalline solids (or, sometimes, glasses) which lack an ordered internal structure and are randomly arranged. Substances that...
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Network Covalent Solids02:18

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Network covalent solids contain a three-dimensional network of covalently bonded atoms as found in the crystal structures of nonmetals like diamond, graphite, silicon, and some covalent compounds, such as silicon dioxide (sand) and silicon carbide (carborundum, the abrasive on sandpaper). Many minerals have networks of covalent bonds.
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Molecular and Ionic Solids02:54

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Crystalline solids are divided into four types: molecular, ionic, metallic, and covalent network based on the type of constituent units and their interparticle interactions.
Molecular Solids
Molecular crystalline solids, such as ice, sucrose (table sugar), and iodine, are solids that are composed of neutral molecules as their constituent units. These molecules are held together by weak intermolecular forces such as London dispersion forces, dipole-dipole interactions, or hydrogen bonds, which...
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Particles in a solid are tightly packed together (fixed shape) and often arranged in a regular pattern; in a liquid, they are close together with no regular arrangement (no fixed shape); in a gas, they are far apart with no regular arrangement (no fixed shape). Particles in a solid vibrate about fixed positions (cannot flow) and do not generally move in relation to one another; in a liquid, they move past each other (can flow) but remain in essentially constant contact; in a gas, they move...
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Monitoring Protein Adsorption with Solid-state Nanopores
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Identifying Single Viruses Using Biorecognition Solid-State Nanopores.

Akihide Arima1, Ilva Hanun Harlisa2, Takeshi Yoshida1

  • 1The Institute of Scientific and Industrial Research , Osaka University , 8-1 Mihogaoka , Ibaraki, Osaka 567-0047 , Japan.

Journal of the American Chemical Society
|November 27, 2018
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Summary

Researchers developed a novel peptide nanopore immunosensor for precise single-virus detection. This technique uses synthetic peptides to identify influenza A virus by altering translocation dynamics, enabling digital typing.

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Area of Science:

  • Biotechnology and Nanotechnology
  • Analytical Chemistry
  • Infectious Disease Diagnostics

Background:

  • Immunosensing relies on specific molecular interactions for pathogen detection.
  • Artificial nanopores offer a platform for single-particle analysis.
  • Developing selective and sensitive biosensors is crucial for disease diagnosis.

Purpose of the Study:

  • To engineer a peptide-based nanopore system for selective identification of single viruses.
  • To utilize synthetic peptides as recognition probes for influenza A virus.
  • To demonstrate digital typing of viruses based on altered translocation dynamics.

Main Methods:

  • Functionalizing artificial nanopore walls with hemagglutinin antibody-mimicking oligopeptides.
  • Investigating the effect of peptide-virus interactions on virus translocation dynamics in a nanochannel.
  • Analyzing resistive pulse signals to differentiate specific viruses.

Main Results:

  • Synthetic peptides conferred specificity to virion-nanopore interactions.
  • Ligand binding perturbed the translocation dynamics of influenza A virus.
  • Digital typing of influenza virus was achieved by analyzing resistive pulse bluntness.

Conclusions:

  • The peptide nanopore approach enables single-particle sensitivity for versatile immunosensing.
  • This method shows potential for broad applications in viral and bacterial screening.
  • The technique promises advancements in infectious disease diagnosis.