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 Single-pass Transmembrane Proteins in the RER01:26

Insertion of Single-pass Transmembrane Proteins in the RER

18.8K
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...
18.8K
Insertion of Multi-pass Transmembrane Proteins in the RER01:29

Insertion of Multi-pass Transmembrane Proteins in the RER

19.5K
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...
19.5K
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

6.8K
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...
6.8K
Protein Transport into the Inner Mitochondrial Membrane01:34

Protein Transport into the Inner Mitochondrial Membrane

5.1K
Nuclear encoded mitochondrial precursors are imported to the inner membrane in a multistep process involving two separate translocons, TIM22 and TIM23. TIM23 is a cation-selective pore that remains closed by the N terminal segment of the protein. Negative charges on the TIM23 act as a receptor for the incoming precursor, pulling the positively charged matrix-targeting sequence for peptide insertion and translocation.
Transport of mitochondrial precursors across the TIM23 channel is driven by...
5.1K
Tail-anchoring of Proteins in the ER Membrane01:45

Tail-anchoring of Proteins in the ER Membrane

4.0K
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...
4.0K

You might also read

Related Articles

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

Sort by
Same author

Cyclosporin A toxicity on endothelial cells differentiated from induced pluripotent stem cells: Assembling an adverse outcome pathway.

Toxicology in vitro : an international journal published in association with BIBRA·2024
Same author

Targeting <i>N</i>-Acetylglucosaminidase in <i>Staphylococcus aureus</i> with Iminosugar Inhibitors.

Antibiotics (Basel, Switzerland)·2024
Same author

Merging Counter-Propagation and Back-Propagation Algorithms: Overcoming the Limitations of Counter-Propagation Neural Network Models.

International journal of molecular sciences·2024
Same author

Exploring the dynamics of the ABCB1 membrane transporter P-glycoprotein in the presence of ATP and active/non-active compounds through molecular dynamics simulations.

Toxicology·2024
Same author

Quantitative Structure Activity/Toxicity Relationship through Neural Networks for Drug Discovery or Regulatory Use.

Current topics in medicinal chemistry·2023
Same author

Cheminformatics and Machine Learning Approaches to Assess Aquatic Toxicity Profiles of Fullerene Derivatives.

International journal of molecular sciences·2023
Same journal

Analysis of strength degradation of coal and rock masses and stability of mined areas under long term immersion environment.

PloS one·2026
Same journal

Biogenic Silver-Selenium nanocomposite with anticancer activity and potent efficacy against vancomycin-resistant Staphylococcus aureus.

PloS one·2026
Same journal

Preparation and physicochemical characterization of a biodegradable chitosan/carboxymethyl cellulose hydrogel synthesized in NaOH/urea medium.

PloS one·2026
Same journal

Action-guilt, survivor-guilt, and depression in combat-related PTSD.

PloS one·2026
Same journal

Explainable machine learning for predicting activities of daily living at discharge in stroke patients: A retrospective study using SHAP interpretability.

PloS one·2026
Same journal

Deep learning based two-way feature depiction model for brain tumor detection.

PloS one·2026
See all related articles

Related Experiment Video

Updated: Mar 28, 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

PredβTM: A Novel β-Transmembrane Region Prediction Algorithm.

Amrita Roy Choudhury1, Marjana Novič1

  • 1Laboratory of Chemometrics, National Institute of Chemistry, Ljubljana, Slovenia.

Plos One
|December 24, 2015
PubMed
Summary
This summary is machine-generated.

PredβTM accurately predicts transmembrane regions in beta-barrel proteins. This new algorithm improves precision and segment overlap compared to existing methods, aiding in understanding protein structures.

More Related Videos

A Protocol for Computer-Based Protein Structure and Function Prediction
16:41

A Protocol for Computer-Based Protein Structure and Function Prediction

Published on: November 3, 2011

70.1K
Determining Membrane Protein Topology Using Fluorescence Protease Protection FPP
08:14

Determining Membrane Protein Topology Using Fluorescence Protease Protection FPP

Published on: April 20, 2015

18.5K

Related Experiment Videos

Last Updated: Mar 28, 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
A Protocol for Computer-Based Protein Structure and Function Prediction
16:41

A Protocol for Computer-Based Protein Structure and Function Prediction

Published on: November 3, 2011

70.1K
Determining Membrane Protein Topology Using Fluorescence Protease Protection FPP
08:14

Determining Membrane Protein Topology Using Fluorescence Protease Protection FPP

Published on: April 20, 2015

18.5K

Area of Science:

  • Biochemistry
  • Structural Biology
  • Bioinformatics

Background:

  • Understanding beta-barrel membrane protein structures is crucial.
  • Current transmembrane region predictors lack sufficient accuracy and precision.
  • Accurate prediction aids in elucidating protein architecture.

Purpose of the Study:

  • To develop a novel algorithm, PredβTM, for predicting transmembrane regions in beta-barrel proteins.
  • To enhance the accuracy and precision of transmembrane region prediction.
  • To identify potential beta-barrel membrane proteins in bacterial genomes.

Main Methods:

  • Utilized amino acid pair frequency information from known beta-transmembrane protein sequences.
  • Trained a support vector machine classifier for segment prediction.
  • Incorporated position-specific amino acid preference data and an amino acid adjacency matrix.

Main Results:

  • PredβTM achieved 83.71% sensitivity and 72.98% precision on a benchmark set of 35 proteins.
  • The algorithm demonstrated a segment overlap score of 82.19%.
  • Outperformed state-of-the-art methods in precision and segment overlap without sacrificing sensitivity.

Conclusions:

  • PredβTM offers improved accuracy for beta-barrel transmembrane region prediction.
  • The algorithm successfully identified potential beta-barrel proteins in bacterial genomes.
  • PredβTM is available as a web server for broader research application.