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Related Concept Videos

Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
Introduction to Membrane Proteins01:16

Introduction to Membrane Proteins

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 types have...
Mitochondrial Precursor Proteins01:39

Mitochondrial Precursor Proteins

Mitochondrial precursors are partially unfolded or loosely folded polypeptide chains. Newly synthesized precursors are inhibited from spontaneously folding into their native conformation by the cytosolic chaperones, heat shock proteins 70 (Hsp70), and mitochondrial import stimulation factors (MSFs). Precursors bound to MSFs are guided to the TOM70-TOM37 receptors, while precursors bound to Hsp70  chaperones are targetted to TOM20-TOM22 receptor complexes.
Most of the mitochondrial precursors...
Membrane Proteins01:30

Membrane Proteins

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...
Membrane Proteins01:30

Membrane Proteins

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...
Single-pass Transmembrane Proteins01:25

Single-pass Transmembrane Proteins

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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Membrane-SPINE: A Biochemical Tool to Identify Protein-protein Interactions of Membrane Proteins In Vivo
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Membrane-SPINE: A Biochemical Tool to Identify Protein-protein Interactions of Membrane Proteins In Vivo

Published on: November 7, 2013

Membrane interacting peptides: from killers to helpers.

Erick J Dufourc1, Sébastien Buchoux, Jeannot Toupé

  • 1Institute of Chemistry & Biology of Membranes & Nanoobjects (CBMN), UMR5248, Université Bordeaux, CNRS Institut Polytechnique Bordeaux, Pessac, France. e.dufourc@iecb.u-bordeaux.fr

Current Protein & Peptide Science
|November 3, 2012
PubMed
Summary

This review explores how various peptides interact with lipid membranes, influencing their function and structure. Certain peptides, like antimicrobial peptides, show potential as new antibiotics by altering membranes.

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Membrane-SPINE: A Biochemical Tool to Identify Protein-protein Interactions of Membrane Proteins In Vivo
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Peptide-based Identification of Functional Motifs and their Binding Partners
14:28

Peptide-based Identification of Functional Motifs and their Binding Partners

Published on: June 30, 2013

Area of Science:

  • Biochemistry and Biophysics
  • Molecular Biology

Background:

  • Peptides interact with lipid membranes, affecting their structure and function.
  • Diverse peptide structures (helical, beta-stranded, cyclic, lipopeptides, linear) modulate membrane properties.
  • Membrane-active peptides include antimicrobial peptides with therapeutic potential.

Purpose of the Study:

  • To review the structure and mechanisms of membrane-interacting peptides.
  • To discuss various models of peptide-lipid complex formation and assembly.
  • To highlight the role of peptides in membrane function and protein activity.

Main Methods:

  • Literature review of studies on peptide-lipid interactions.
  • Analysis of peptide structures and their modes of action on membranes.
  • Discussion of established models for peptide-induced membrane alterations.

Main Results:

  • Peptides significantly modulate membrane function through diverse structural interactions.
  • Antimicrobial peptides are key effectors of membrane alteration and potential antibiotics.
  • Non-lytic peptides are crucial for regulating lipid bilayer dynamics and membrane protein function.

Conclusions:

  • Peptide-lipid complexes exhibit variable structures and dynamics.
  • Models like 'carpet,' 'barrel stave,' and electroporation explain peptide-induced membrane changes.
  • Peptide assembly depends on the physicochemical properties of both peptides and lipids.