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Related Concept Videos

Multi-pass Transmembrane Proteins and β-barrels01:09

Multi-pass Transmembrane Proteins and β-barrels

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In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
α-Helix containing multi-pass transmembrane proteins
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Introduction to Membrane Proteins01:16

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The cell membrane, or plasma membrane, is an ever-changing landscape. It is described as a fluid mosaic where various macromolecules are embedded in the phospholipid bilayer. Among the macromolecules are proteins. The protein content varies across cell types. For example, mitochondrial inner membranes contain ~76% protein content, while myelin contains ~18% protein content. Individual cells contain many types of membrane proteins—red blood cells contain over 50—and different cell...
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Membrane Proteins01:30

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Plasma membranes have integral transmembrane proteins involved in facilitated transport. These proteins are collectively referred to as transport proteins, and they function as either channels for the material or as carriers themselves. Channel proteins have hydrophilic domains exposed to the intracellular and extracellular fluids and a hydrophilic channel through their core that provides a hydrated opening for solutes to pass through the membrane layers. Passage through the channel allows...
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Integral membrane proteins are tightly associated with the cell membrane and play a crucial role in cell communication, signaling, adhesion, and transport of the molecules. Some integral membrane proteins are present only in the membrane monolayer. For example, the enzyme fatty acid amide hydrolase is present in the cytoplasmic side of the membrane monolayer. In contrast, another type of integral membrane protein, also known as a transmembrane protein, spans across the membrane. Transmembrane...
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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...
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Viral Structure00:56

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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.
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Membrane binding proteins of coronaviruses.

Entedar A J Alsaadi1,2,1,2, Ian M Jones1,1

  • 1Biomedical Sciences, School of Biological Sciences, University of Reading, Reading RG6 6AJ, UK.

Future Virology
|March 24, 2020
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Coronaviruses (CoVs) utilize host cell membranes for replication. This study details how viral proteins bind and remodel membranes, crucial for understanding coronavirus infection and developing therapies.

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bendingcoronavirusegressfusionmembranepeptidereplicationweb

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Area of Science:

  • Virology
  • Cell Biology
  • Molecular Biology

Background:

  • Coronaviruses (CoVs) cause diverse diseases and include pandemic threats with limited treatments.
  • CoVs manipulate host cell membranes, creating structures vital for their replication cycle.

Purpose of the Study:

  • To comprehensively describe the membrane-binding roles of individual coronavirus proteins.
  • To elucidate how viral proteins interact with and reorganize cellular membranes during infection.

Main Methods:

  • Review and synthesis of existing literature on coronavirus protein-membrane interactions.
  • Analysis of the functions of structural and nonstructural viral proteins in membrane binding.

Main Results:

  • Both structural and nonstructural CoV proteins possess membrane-binding properties.
  • Structural proteins interact with membranes during viral entry and exit.
  • Nonstructural proteins actively reorganize cellular membranes to facilitate viral replication.

Conclusions:

  • Understanding CoV protein-membrane interactions is key to comprehending the viral lifecycle.
  • Targeting these interactions may offer novel therapeutic strategies against coronavirus infections.