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

Mechanisms of Membrane-bending01:15

Mechanisms of Membrane-bending

The living membranes are flexible due to their fluid mosaic nature; however, their bending into different shapes is an active process regulated by specific lipids and proteins. The membrane bending can be transient as seen in vesicles or stable for a long time as in microvilli. Cells regulate the size, location, and duration of the membrane curvature.
Membrane bending can happen due to intrinsic changes in lipid composition or extrinsic association with different proteins. The proteins involved...
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...
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...
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...
Membrane Fluidity01:23

Membrane Fluidity

Cell membranes are composed of phospholipids, proteins, and carbohydrates loosely attached to one another through chemical interactions. Molecules are generally able to move about in the plane of the membrane, giving the membrane its flexible nature called fluidity. Two other features of the membrane contribute to membrane fluidity: the chemical structure of the phospholipids and the presence of cholesterol in the membrane.
Membrane Fluidity01:26

Membrane Fluidity

Membrane fluidity is explained by the fluid mosaic model of the cell membrane, which describes the plasma membrane structure as a mosaic of components—including phospholipids, cholesterol, proteins, and carbohydrates—that gives the membrane a fluid character.
Mosaic nature of the membrane
The mosaic characteristic of the membrane helps the plasma membrane remain fluid. The integral proteins and lipids exist as separate but loosely-attached molecules in the membrane. The membrane is a relatively...

You might also read

Related Articles

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

Sort by
Same author

EGFR endocytosis down-regulates binding to EphA2 at the plasma membrane.

The Journal of biological chemistry·2026
Same author

[<sup>64</sup>Cu]Cu-DOTA-TYPE7: a targeted PET radiotracer for imaging EphA2+ tumors.

Npj imaging·2026
Same author

Screening the Human Proteome for Peptides Targeting the Acidic Environment of Tumor Tissues.

Chemical & pharmaceutical bulletin·2026
Same author

SiMPull-POP: Quantification of Membrane Protein Assembly via Single Molecule Photobleaching.

Bio-protocol·2026
Same author

Rapid and improved surface passivation method for Single-Molecule experiments.

Methods (San Diego, Calif.)·2026
Same author

Cholesterol promotes the formation of dimers and oligomers of the receptor tyrosine kinase ROR1.

The Journal of biological chemistry·2025
Same journal

Chemotactic self-organization captures the dynamics of mammalian hair follicle patterning.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same journal

Tomographic imaging of superconducting order using particle-hole interference.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same journal

Inhibitory potential of autologous neutralizing antibodies sets quantitative limits on the rebound-competent HIV-1 reservoir.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same journal

Inferring epidemiological parameters under an infectious phylogeography model with visitor dynamics.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same journal

Analytical modeling for suction cup designs for skin-interfaced wearable devices.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same journal

Improving cell-free metabolism through direct integration of artificial respiratory chains.

Proceedings of the National Academy of Sciences of the United States of America·2026
See all related articles

Related Experiment Video

Updated: May 19, 2026

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
06:45

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay

Published on: May 26, 2011

Membrane physical properties influence transmembrane helix formation.

Francisco N Barrera1, Justin Fendos, Donald M Engelman

  • 1Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA.

Proceedings of the National Academy of Sciences of the United States of America
|August 22, 2012
PubMed
Summary
This summary is machine-generated.

The pH-Low Insertion Peptide (pHLIP) inserts into cell membranes at acidic pH, enabling targeted delivery to diseases like cancer. Membrane properties influence its insertion, suggesting potential for improved tumor targeting strategies.

More Related Videos

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

Pulling Membrane Nanotubes from Giant Unilamellar Vesicles
06:26

Pulling Membrane Nanotubes from Giant Unilamellar Vesicles

Published on: December 7, 2017

Related Experiment Videos

Last Updated: May 19, 2026

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
06:45

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay

Published on: May 26, 2011

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

Pulling Membrane Nanotubes from Giant Unilamellar Vesicles
06:26

Pulling Membrane Nanotubes from Giant Unilamellar Vesicles

Published on: December 7, 2017

Area of Science:

  • Biophysics
  • Membrane protein interactions
  • Peptide science

Background:

  • The pH-Low Insertion Peptide (pHLIP) transitions between soluble, surface-bound, and transmembrane states.
  • Low pH triggers pHLIP insertion, offering potential for targeting acidic disease microenvironments like tumors.

Purpose of the Study:

  • Investigate how lipid bilayer properties influence pHLIP's membrane insertion.
  • Determine the role of peptide conformation and membrane physics in transmembrane helix formation.

Main Methods:

  • Studied pHLIP states using varying lipid acyl chain lengths and cholesterol concentrations.
  • Utilized a cell insertion assay to determine membrane insertion pKa in live cells.
  • Analyzed the impact of the P20G variant on pHLIP's alpha-helix content.

Main Results:

  • pHLIP's bound state helicity correlates with lipid acyl chain length, suggesting bilayer elastic bending modulus influence.
  • Membrane insertion pKa exhibits a biphasic dependence on membrane physical properties.
  • Proline residue in pHLIP variant (P20G) decreases alpha-helix content in both bound and inserted states.
  • pHLIP's behavior in liposomes mirrors that within complex plasma membranes.

Conclusions:

  • Peptide conformational propensities and bilayer physical properties jointly modulate transmembrane helix formation.
  • Altered membrane fluidity in tumor cells may impact pHLIP tumor targeting efficacy.
  • Helix-membrane interactions play a physical role in optimizing complex transmembrane protein function.