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Related Concept Videos

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...
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...
Multi-pass Transmembrane Proteins and β-barrels01:09

Multi-pass Transmembrane Proteins and β-barrels

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
Multi-pass transmembrane proteins such as G-protein-linked receptors (GPCRs) and...
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...
Insertion of Multi-pass Transmembrane Proteins in the RER01:29

Insertion of Multi-pass Transmembrane Proteins in the RER

The rough ER membrane synthesizes, assembles, and embeds transmembrane proteins in diverse topologies. These proteins function as transporters or channels and can remain in the ER membrane or are sent to the Golgi complex, lysosome, and cell membrane.
The multipass transmembrane proteins are the type IV integral membrane proteins with multiple topogenic sequences determining their spatial arrangement in the ER membrane. Nearly all multipass proteins lack a cleavable signal sequence and use...

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Updated: May 26, 2026

Determination of Plasma Membrane Partitioning for Peripherally-associated Proteins
11:11

Determination of Plasma Membrane Partitioning for Peripherally-associated Proteins

Published on: June 15, 2018

Conditional peripheral membrane proteins: facing up to limited specificity.

Katarina Moravcevic1, Camilla L Oxley, Mark A Lemmon

  • 1Department of Biochemistry and Biophysics, University of Pennsylvania Perelman School of Medicine, Philadelphia, PA 19104, USA.

Structure (London, England : 1993)
|December 24, 2011
PubMed
Summary
This summary is machine-generated.

Cellular protein movement relies on specialized domains that bind membrane components. Recent discoveries show these domains often bind multiple targets, posing new research challenges.

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The C. elegans Intestine As a Model for Intercellular Lumen Morphogenesis and In Vivo Polarized Membrane Biogenesis at the Single-cell Level: Labeling by Antibody Staining, RNAi Loss-of-function Analysis and Imaging
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Published on: August 10, 2021

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Regulated protein relocalization is vital for cellular processes.
  • Early identified domains (C1, C2, PH, PX, FYVE) specifically bind membrane components like phosphoinositides.
  • The structural basis for these specific interactions is well-understood.

Purpose of the Study:

  • To investigate newly discovered conditional peripheral membrane proteins.
  • To understand their target recognition mechanisms beyond specific phospholipid binding.
  • To address the challenges in structurally characterizing proteins with broader recognition modes.

Main Methods:

  • Literature review of recent discoveries in conditional peripheral membrane proteins.
  • Analysis of reported binding specificities and recognition mechanisms.
  • Identification of methodological challenges in structural biology.

Main Results:

  • Few new specific phospholipid-binding domains have been identified.
  • Most novel proteins bind multiple targets with limited specificity.
  • Recognition often involves coincidence detection or broader membrane properties (charge, curvature).

Conclusions:

  • Conditional peripheral membrane proteins exhibit diverse recognition strategies.
  • Understanding these complex interactions requires new structural and biophysical approaches.
  • This shift challenges traditional views of specific molecular recognition at membranes.