Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Insertion of Multi-pass Transmembrane Proteins in the RER01:29

Insertion of Multi-pass Transmembrane Proteins in the RER

19.6K
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...
19.6K
Insertion of Single-pass Transmembrane Proteins in the RER01:26

Insertion of Single-pass Transmembrane Proteins in the RER

18.9K
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...
18.9K
Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

21.7K
Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
21.7K
Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

3.0K
3.0K
Single-pass Transmembrane Proteins01:25

Single-pass Transmembrane Proteins

7.1K
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...
7.1K
Multi-pass Transmembrane Proteins and β-barrels01:09

Multi-pass Transmembrane Proteins and β-barrels

6.9K
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...
6.9K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Decoding the Apical-Basal Surfaceome of Colon Epithelial Cells via Side-Selective Biotinylation.

Biomolecules·2026
Same author

Toward a unified framework for determining conformational ensembles of disordered proteins.

Nature methods·2026
Same author

Frag'n'Flow: automated workflow for large-scale quantitative proteomics in high performance computing environments.

BMC bioinformatics·2026
Same author

Definition and Discovery of Tandem SH3-Binding Motifs Interacting with Members of the p47<sup>phox</sup>-Related Protein Family.

Biomolecules·2025
Same author

Optimization of Methods for the Quantitative Analysis of Global Cell Surface Proteome and Cell Surface Polarization.

International journal of molecular sciences·2025
Same author

Expression, purification, and biophysical characterization of liquid-liquid phase separation of full-length hnRNPA2B1.

Protein expression and purification·2025
Same journal

Cumulative Contents.

Biochimica et biophysica acta·2020
Same journal

Molecular Basis of Disease Cumulative Contents.

Biochimica et biophysica acta·2020
Same journal

General Subjects Cumulative Contents.

Biochimica et biophysica acta·2020
Same journal

Erratum to 'on the role of exchangeable hydrogen bonds for the kinetics of P680<sup>+·</sup> Q<sub>A</sub> <sup>-·</sup> formation and P680<sup>+·</sup> Pheo<sup>-·</sup> recombination in photosystem II' [Biochim. Biophys. Acta 1276 (1996) 35-44].

Biochimica et biophysica acta·2019
Same journal

Oligomeric state of the light-harvesting complexes B800-850 and B875 from purple bacterium Rubrivivax gelatinosus in detergent solution.

Biochimica et biophysica acta·2019
Same journal

Regulation of pigment content and enzyme activity in the cyanobacterium Nostoc sp. Mac grown in continuous light, a light-dark photoperiod, or darkness.

Biochimica et biophysica acta·2019
See all related articles

Related Experiment Video

Updated: Apr 5, 2026

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
06:45

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay

Published on: May 26, 2011

15.8K

Disordered regions in transmembrane proteins.

Gábor E Tusnády1, László Dobson1, Peter Tompa2

  • 1Institute of Enzymology, RCNS, HAS, Magyar Tudósok körútja 2, 1117 Budapest, Hungary.

Biochimica Et Biophysica Acta
|August 16, 2015
PubMed
Summary
This summary is machine-generated.

Transmembrane proteins have disordered regions that correlate with charged residues, suggesting a role in stabilizing lipid interactions. Disorder is preferred in terminal regions, impacting protein recruitment and signaling.

Keywords:
Intrinsically disordered residuesPositive inside rulePredictionTopologyTransmembrane protein

More Related Videos

Reconstitution of Msp1 Extraction Activity with Fully Purified Components
05:52

Reconstitution of Msp1 Extraction Activity with Fully Purified Components

Published on: August 10, 2021

3.0K
Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies
12:05

Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies

Published on: March 6, 2013

14.7K

Related Experiment Videos

Last Updated: Apr 5, 2026

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
06:45

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay

Published on: May 26, 2011

15.8K
Reconstitution of Msp1 Extraction Activity with Fully Purified Components
05:52

Reconstitution of Msp1 Extraction Activity with Fully Purified Components

Published on: August 10, 2021

3.0K
Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies
12:05

Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies

Published on: March 6, 2013

14.7K

Area of Science:

  • Biochemistry
  • Structural Biology
  • Cell Biology

Background:

  • Transmembrane proteins perform vital cellular functions, including transport, energy production, cell adhesion, and communication.
  • These proteins exhibit ordered membrane-spanning regions but can possess disordered regions in their extracellular and cytosolic domains.

Purpose of the Study:

  • To investigate the characteristics and functions of disordered regions within transmembrane proteins.
  • To establish a correlation between the distribution of charged residues and disordered regions in transmembrane proteins.
  • To evaluate the performance of various disorder prediction methods for transmembrane proteins.

Main Methods:

  • Utilized the largest available experimental dataset of transmembrane proteins.
  • Applied a stringent definition to identify disordered residues.
  • Analyzed the spatial distribution of charged residues and disordered regions.
  • Compared the efficacy of different computational disorder prediction tools.

Main Results:

  • A significant correlation was found between the spatial distribution of positively charged residues and disordered regions in transmembrane proteins.
  • Disordered regions in transmembrane proteins may play a role in stabilizing interactions with negatively charged lipid head groups.
  • Structural disorder is preferentially located in the terminal regions, rather than loop regions, of transmembrane proteins, influencing protein recruitment and allosteric signaling.

Conclusions:

  • Disordered regions in transmembrane proteins contribute to structural flexibility and interaction with membrane lipids.
  • Terminal disordered regions are functionally significant for protein interactions and signaling pathways.
  • Development of a disorder predictor specifically optimized for transmembrane proteins is highly valuable for structural biology research.