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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...
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...
Conserved Binding Sites01:49

Conserved Binding Sites

Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...
Conserved Binding Sites01:49

Conserved Binding Sites

Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...

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Related Experiment Video

Updated: Jul 4, 2026

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

Coils in the membrane core are conserved and functionally important.

Anni Kauko1, Kristoffer Illergård, Arne Elofsson

  • 1Center for Biomembrane Research, Stockholm University, SE-106 91 Stockholm, Sweden.

Journal of Molecular Biology
|May 31, 2008
PubMed
Summary

Coil residues in the membrane core, though structurally unusual, are crucial for protein function. These conserved residues provide essential flexibility and polarity for transport across cell membranes.

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Reconstitution of a Kv Channel into Lipid Membranes for Structural and Functional Studies
10:22

Reconstitution of a Kv Channel into Lipid Membranes for Structural and Functional Studies

Published on: July 13, 2013

Related Experiment Videos

Last Updated: Jul 4, 2026

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

Reconstitution of a Kv Channel into Lipid Membranes for Structural and Functional Studies
10:22

Reconstitution of a Kv Channel into Lipid Membranes for Structural and Functional Studies

Published on: July 13, 2013

Area of Science:

  • Biochemistry
  • Structural Biology
  • Membrane Protein Research

Background:

  • Traditional models of alpha-helical transmembrane (TM) proteins are evolving with new structural data.
  • Unconventional structures like reentrant regions and interface helices are increasingly recognized.
  • TM helices exhibit variability in kinks, length, and tilt angles.

Purpose of the Study:

  • To systematically analyze coil residues located in the deep membrane core.
  • To understand the structural roles and functional significance of these coil residues.
  • To investigate the conservation patterns and localization of coil residues.

Main Methods:

  • Bioinformatic analysis of TM protein structures.
  • Identification and characterization of coil residues within the membrane core.
  • Assessment of residue conservation and localization relative to aqueous environments.

Main Results:

  • Coil residues constitute 7% of residues in the deep membrane core.
  • Coils are prevalent in TM-helix kinks and reentrant regions.
  • Coil residues are significantly more conserved and often found near or within aqueous channels.

Conclusions:

  • Coil residues in the membrane core, despite being a structural anomaly, are vital for protein function.
  • Their polar backbone and location facilitate flexibility and polarity necessary for membrane transport.
  • These residues play a key role in the function of channels and transporters.