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Related Concept Videos

Membrane Domains01:18

Membrane Domains

The membrane domains concentrate specific lipids and proteins at one place within the membrane, which helps in cell signaling, adhesion, and other critical cellular processes. These domains can differ in size, composition, function, and lifespan.
Protein Domains
The membrane comprises a group of distinct proteins responsible for carrying out a cell's specific function. For example, the plasma membrane of the human sperm, or a single germ cell, contains a unique set of proteins in the anterior...
Mechanisms of Membrane Domain Formation00:59

Mechanisms of Membrane Domain Formation

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.
Another mechanism for membrane domain formation involves membrane proteins interacting with cytoskeletal...
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...
Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
Fluid Mosaic Model01:19

Fluid Mosaic Model

Scientists identified the plasma membrane in the 1890s and its principal chemical components (lipids and proteins) by 1915. The model for plasma membrane structure, proposed in 1935 by Hugh Davson and James Danielli, was the first model to be widely accepted in the scientific community. The model was based on the plasma membrane's "railroad track" appearance in early electron micrographs. Davson and Danielli theorized that the plasma membrane's structure resembled a sandwich with the analogy of...
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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Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy
10:49

Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy

Published on: March 5, 2017

Protein structure in membrane domains.

Arianna Rath1, Charles M Deber

  • 1Division of Molecular Structure & Function, Research Institute, Hospital for Sick Children, Toronto, Ontario, M5G 1X8, Canada.

Annual Review of Biophysics
|May 15, 2012
PubMed
Summary
This summary is machine-generated.

This review explores how helical transmembrane domains (TMDs) fold and interact within lipid bilayers, focusing on the crucial role of membrane-mimetic solvents in understanding their structure and stability.

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Contrast-Matching Detergent in Small-Angle Neutron Scattering Experiments for Membrane Protein Structural Analysis and Ab Initio Modeling

Published on: October 21, 2018

Area of Science:

  • Biochemistry
  • Structural Biology
  • Membrane Protein Research

Background:

  • Helical transmembrane proteins are vital in biological systems and drug development.
  • Their function relies on transmembrane domains (TMDs) that integrate into lipid bilayers.
  • Studying TMDs requires specialized membrane-mimetic solvents due to their apolar nature.

Purpose of the Study:

  • To review the relationship between transmembrane domain (TMD) structure and solvent environment.
  • To highlight principles derived from studies using single-TMD protein and peptide models in membrane-mimetic settings.
  • To discuss factors influencing TMD incorporation, self-assembly, and stability.

Main Methods:

  • Analysis of sequence and conformational characteristics from structural databases.
  • Overview of conceptual models for in vitro folding studies.
  • Examination of experimental data on TMDs in membrane-mimetic solvents.

Main Results:

  • TMD sequence and solvent context significantly impact membrane incorporation and self-assembly.
  • Membrane-mimetic environments provide valuable insights into TMD folding principles.
  • Non-specific effects of membrane components can influence TMD stability.

Conclusions:

  • Understanding TMD structure-function relationships is critical for pharmaceutical research.
  • Membrane-mimetic solvents are essential tools for studying transmembrane protein folding.
  • Further investigation into the influence of the membrane environment on TMD stability is warranted.