Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Asymmetric Lipid Bilayer

Asymmetric Lipid Bilayer

Biological membranes show uneven distribution of different types of lipids in the inner and outer layers, resulting in transverse asymmetric membranes. The treatment of the erythrocyte membrane with the enzyme phospholipase confirmed the asymmetric nature of the lipid bilayer. The enzyme hydrolyzes lipids into fatty acids and hydrophilic groups. The phospholipase acts only on the outer layer of the membrane, while the inner layer remains intact. The phospholipase treatment resulted in 80%...

Protein-protein Interfaces

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...

SNAREs and Membrane Fusion

SNAREs and Membrane Fusion

Once a transport vesicle has recognized its target organelle, the vesicular membrane needs to fuse with the target membrane to unload the cargo. Transmembrane proteins called SNAREs present on organelle membranes and their vesicles, mediate vesicle fusion.
SNAREs exist in pairs that symmetrically interact and catalyze the fusion of the lipid bilayers in vesicle and target organelle. v-SNARE in the vesicle membrane are single polypeptide chains that bind to a complementary t-SNARE, composed of 2...

Membrane Domains

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...

Membrane Fluidity

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...

Fluid Mosaic Model

Fluid Mosaic Model

The fluid mosaic model was first proposed as a visual representation of research observations. The model comprises the composition and dynamics of membranes and serves as a foundation for future membrane-related studies. The model depicts the structure of the plasma membrane with a variety of components, which include phospholipids, proteins, and carbohydrates. These integral molecules are loosely bound, defining the cell’s border and providing fluidity for optimal function.LipidsThe most...

You might also read

Related Articles

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

Sort by

Same author

School zone speed compliance in the ACT, Australia: Risks, findings and recommendations for improved safety.

Journal of safety research·2026

Same author

Effect of [<sup>68</sup>Ga]Ga-PSMA-11 PET-CT in the diagnosis of prostate cancer in men with equivocal or clinically high-risk non-suspicious findings on multiparametric MRI (PRIMARY2): a multicentre, non-inferiority, phase 3, randomised controlled trial.

The Lancet. Oncology·2026

Same author

Tubule and microbranch variations in human dentine: A quantitative 3D study with serial block-face scanning electron microscopy.

Journal of microscopy·2026

Same author

An AI system to help scientists write expert-level empirical software.

Nature·2026

Same author

Prospective Comparison of <sup>64</sup>Copper [<sup>64</sup>Cu]SAR-bisPSMA vs <sup>68</sup>Gallium[<sup>68</sup>Ga] PSMA-11 PET/CT for Biochemical Recurrence of Prostate Cancer Following Radical Prostatectomy (Co-PSMA Trial).

European urology·2026

Same author

Characteristics of Patients and Factors Associated With the Development of Hepatitis C Virus-Associated Hepatocellular Carcinoma in an Urban, Primary-Care Based Hepatitis C Clinic.

Journal of viral hepatitis·2026

Same journal

Imbalance in amino acid and purine metabolisms at the hypothalamus in inflammation-associated depression by GC-MS.

Molecular bioSystems·2017

Same journal

Correction: Dynamic properties of dipeptidyl peptidase III from Bacteroides thetaiotaomicron and the structural basis for its substrate specificity - a computational study.

Molecular bioSystems·2017

Same journal

Conformational heterogeneity in tails of DNA-binding proteins is augmented by proline containing repeats.

Molecular bioSystems·2017

Same journal

Mechanism of the formation of the RecA-ssDNA nucleoprotein filament structure: a coarse-grained approach.

Molecular bioSystems·2017

Same journal

Staphylococcus aureus extracellular vesicles (EVs): surface-binding antagonists of biofilm formation.

Molecular bioSystems·2017

Same journal

Development of an AlphaLISA high throughput technique to screen for small molecule inhibitors targeting protein arginine methyltransferases.

Molecular bioSystems·2017

See all related articles

Search research articles

Related Experiment Video

Updated: Jun 23, 2026

Temperature-Controlled Assembly and Characterization of a Droplet Interface Bilayer

Temperature-Controlled Assembly and Characterization of a Droplet Interface Bilayer

Published on: April 19, 2021

Droplet interface bilayers.

Hagan Bayley¹, Brid Cronin, Andrew Heron

¹Department of Chemistry, University of Oxford, Oxford, UK. hagan.bayley@chem.ox.ac.uk

Molecular Biosystems

|April 28, 2009

Summary

This summary is machine-generated.

Droplet interface bilayers (DIBs) offer an advanced method for studying membrane proteins. These versatile DIBs can also create networks with integrated power and sensing capabilities.

More Related Videos

Multifunctional, Micropipette-based Method for Incorporation And Stimulation of Bacterial Mechanosensitive Ion Channels in Droplet Interface Bilayers

Multifunctional, Micropipette-based Method for Incorporation And Stimulation of Bacterial Mechanosensitive Ion Channels in Droplet Interface Bilayers

Published on: November 19, 2015

Related Experiment Videos

Last Updated: Jun 23, 2026

Temperature-Controlled Assembly and Characterization of a Droplet Interface Bilayer

Temperature-Controlled Assembly and Characterization of a Droplet Interface Bilayer

Published on: April 19, 2021

Multifunctional, Micropipette-based Method for Incorporation And Stimulation of Bacterial Mechanosensitive Ion Channels in Droplet Interface Bilayers

Multifunctional, Micropipette-based Method for Incorporation And Stimulation of Bacterial Mechanosensitive Ion Channels in Droplet Interface Bilayers

Published on: November 19, 2015

Area of Science:

Biophysics
Materials Science
Biotechnology

Background:

Membrane proteins are crucial for cellular functions.
Studying membrane proteins requires advanced biophysical techniques.
Droplet interface bilayers (DIBs) present a novel platform for such studies.

Purpose of the Study:

To highlight the utility of DIBs in biophysical analysis of membrane proteins.
To explore the potential of DIBs in forming complex networks.
To showcase the integrated functionalities of DIBs, such as built-in batteries and sensors.

Main Methods:

Formation and manipulation of droplet interface bilayers.
Biophysical characterization of membrane proteins within DIBs.
Assembly of interconnected DIB networks.

Main Results:

DIBs demonstrate superior performance for membrane protein analysis.
Successful formation of DIB networks with tunable properties.
Demonstration of integrated battery and sensor functionalities within DIB networks.

Conclusions:

DIBs are a versatile and powerful platform for membrane protein research.
DIB networks offer new possibilities for bioelectronic devices.
The integrated features of DIBs open avenues for advanced biosensing and energy applications.