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Related Concept Videos

Peptide Bonds02:43

Peptide Bonds

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A peptide bond covalently attaches amino acids through a dehydration reaction. One amino acid's carboxyl group and another amino acid's amino group combine, releasing a water molecule. The resulting bond is the peptide bond. The products that such linkages form are peptides. As more amino acids join this growing chain, the resulting chain is a polypeptide. Each polypeptide has a free amino group at one end. This end has the N-terminal, or the amino-terminal, and the other end has a free...
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Multi-pass Transmembrane Proteins and β-barrels01:09

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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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Single-pass Transmembrane Proteins01:25

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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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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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Lipids as Anchors01:32

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In the plasma membrane, the lipids forming the bilayer can also act as an anchor to tether proteins to the membrane. The three main types of lipid anchors found in eukaryotes are – prenyl groups, fatty acyl groups, and glycosylphosphatidylinositol or GPI groups. Prenyl and fatty acyl groups act as anchors on the cytosolic surface of the membrane, whereas GPI anchors proteins on the extracellular side.
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Different physical properties of lipids and proteins allow them to localize and form distinct islands or domains in the membrane. Some membrane domains are formed due to protein-protein interactions, whereas others are formed due to the presence of specific lipids such as sphingolipids and sterols—for example, large proteins, such as bacteriorhodopsin, aggregate and create distinct domains.
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Fluorescent Leakage Assay to Investigate Membrane Destabilization by Cell-Penetrating Peptide
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Concluding remarks: peptide-membrane interactions.

Patricia Bassereau1

  • 1Institut Curie, Université PSL, Sorbonne Université, CNRS UMR168, Laboratoire Physico-Chimie Curie, 75005 Paris, France. patricia.bassereau@curie.fr.

Faraday Discussions
|November 26, 2021
PubMed
Summary
This summary is machine-generated.

This lecture summarizes key findings on peptide-membrane interactions discussed at a 2021 Faraday Discussion meeting. It highlights advancements in understanding how peptides interact with cell membranes.

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Area of Science:

  • Biochemistry
  • Biophysics
  • Molecular Biology

Background:

  • Peptide-membrane interactions are crucial for various biological processes.
  • Understanding these interactions is key to developing new therapeutics.

Purpose of the Study:

  • To summarize the main themes and findings from the Faraday Discussion meeting on peptide-membrane interactions.
  • To highlight recent advancements and future directions in the field.

Main Methods:

  • The article is based on a lecture summarizing discussions from a virtual meeting.
  • Key research findings and methodologies were presented and debated by experts.

Main Results:

  • Significant progress has been made in characterizing peptide binding and insertion into membranes.
  • New insights into the role of membrane composition and dynamics were discussed.

Conclusions:

  • The field of peptide-membrane interactions is rapidly evolving with new experimental and computational approaches.
  • Further research is needed to fully elucidate the complexities of these interactions and their biological implications.