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Related Concept Videos

The Inner Mitochondrial Membrane01:28

The Inner Mitochondrial Membrane

The inner mitochondrial membrane is the primary site of ATP synthesis. The inner membrane domain that forms a smooth layer adjacent to the outer membrane is called the inner boundary membrane. This domain contains membrane transporters that drive metabolites in and out of the mitochondria.  In contrast, the inner membrane network that invaginates into the matrix space is called the cristae membrane. This domain accounts for principle mitochondrial function as it accommodates the protein...
Porin Insertion in the Outer Mitochondrial Membrane01:12

Porin Insertion in the Outer Mitochondrial Membrane

Porins are beta-barrel proteins translocated to the mitochondrial outer membrane through the TOM complex into the intermembrane space. Porin precursors bind TIM chaperones within the intermembrane space and are guided to the Sorting and Assembly Machinery complex or SAM complex on the outer mitochondrial membrane.
Three models describe the assembly of porins by the SAM complex and their insertion into the outer membrane. Model 1 suggests that porins are assembled outside the SAM channel as the...
Insertion of Single-pass Transmembrane Proteins in the RER01:26

Insertion of Single-pass Transmembrane Proteins in the RER

Integral membrane proteins are proteins adhered to the lipid bilayer of a cell organelle or membrane. They can be of two types: transmembrane integral proteins that span the lipid bilayer and monotopic proteins that are attached to either side of the membrane but do not pass through it.
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...
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...
Tail-anchoring of Proteins in the ER Membrane01:45

Tail-anchoring of Proteins in the ER Membrane

Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
Structure of Porins01:21

Structure of Porins

Mitochondria, chloroplasts, and gram-negative bacteria have transmembrane, beta-barrel proteins called porins to mediate the free diffusion of ions and metabolites across the membrane. Mitochondrial porin precursors contain conserved amino acid sequences called beta signals at their C-terminal. Beta signals have a  motif of PoXGXXHyXHy (Po-Polar, X-Any amino acid, G-Glycine, Hy-LargeHydrophobic), which are crucial for precursor recognition to initiate precursor assembly. Beta-barrel precursors...

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Related Experiment Video

Updated: Jul 17, 2026

Examining the Conformational Dynamics of Membrane Proteins in situ with Site-directed Fluorescence Labeling
11:55

Examining the Conformational Dynamics of Membrane Proteins in situ with Site-directed Fluorescence Labeling

Published on: May 29, 2011

In vitro membrane-inserted conformation of the cytochrome b(5) tail.

M R Hanlon1, R R Begum, R J Newbold

  • 1Department of Crystallography, Birkbeck College, University of London, London WC1E 7HX, UK.

The Biochemical Journal
|November 4, 2000
PubMed
Summary

The cytochrome b(5) tail, an endoplasmic reticulum membrane anchor, is likely a single transmembrane helix, not a helical hairpin. Temperature changes increase helical content in lipid environments.

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In Vitro Reconstitution of Self-Organizing Protein Patterns on Supported Lipid Bilayers

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Last Updated: Jul 17, 2026

Examining the Conformational Dynamics of Membrane Proteins in situ with Site-directed Fluorescence Labeling
11:55

Examining the Conformational Dynamics of Membrane Proteins in situ with Site-directed Fluorescence Labeling

Published on: May 29, 2011

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

Published on: March 5, 2017

In Vitro Reconstitution of Self-Organizing Protein Patterns on Supported Lipid Bilayers
08:10

In Vitro Reconstitution of Self-Organizing Protein Patterns on Supported Lipid Bilayers

Published on: July 28, 2018

Area of Science:

  • Biochemistry
  • Membrane Biology
  • Protein Structure

Background:

  • The cytochrome b(5) tail anchors its catalytic domain to the endoplasmic reticulum membrane.
  • Proposed models for the tail's structure include a helical hairpin or a single transmembrane helix.

Purpose of the Study:

  • To investigate the conformation of the cytochrome b(5) tail in various environments and temperatures.
  • To determine the nature of the membrane-bound conformation of the cytochrome b(5) tail.

Main Methods:

  • Circular dichroism (CD) spectroscopy was employed.
  • Experiments were conducted in small unilamellar vesicles and lysophosphatidylcholine micelles.
  • Residue property profiling was used to analyze potential helix bending.

Main Results:

  • Experimental data favor a single transmembrane helix model over a helical hairpin.
  • Temperature-dependent refolding suggests increased helical content in fluid lipid environments.
  • This refolding is not indicative of a hairpin-to-transmembrane transition.

Conclusions:

  • The cytochrome b(5) tail adopts a single transmembrane helix conformation.
  • Lipid environment and temperature influence the helical content and stability of the tail.