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

Fusion of Secretory Vesicles with the Plasma Membrane

Fusion of Secretory Vesicles with the Plasma Membrane

Proteins and neurotransmitters in secretory vesicles can be released from a cell upon vesicle docking, priming, and fusion with the plasma membrane. Vesicles are docked and primed in preparation for the quick exocytosis of their contents in response to a stimulus. The fusion process is mainly carried out by a SNAP Receptor or SNARE complex, consisting of synaptobrevin, syntaxin-1, and SNAP-25.
In 1993, Jim Rothman proposed that the antiparallel pairing of vesicular and transmembrane SNAREs, or...

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...

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...

Tagging and Fusion Proteins

Tagging and Fusion Proteins

Proteins are involved in several cellular processes and biochemical reactions. Analyzing a specific protein of interest requires it to be isolated from the other proteins in the cell. This is achieved by overexpressing the specific gene in a suitable host to produce large quantities of the target protein. A tag or label is recombined with the gene to produce a fusion protein containing the target protein and the tag. The tags on these fusion proteins can then be used for easy detection and...

Protein Complexes with Interchangeable Parts

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...

You might also read

Related Articles

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

Sort by

Same author

Steric Control of Cooperative Anion Transport Mediated by β- and δ‑Hexachlorocyclohexane Multivalent Carriers.

JACS Au·2026

Same author

Dynamic Regulation of Proton and Water Transport through an Acylhydrazone-Based Photoresponsive Channel.

Journal of the American Chemical Society·2025

Same author

State-Dependent Dynamic Communication Networks in a Pentameric Ligand-Gated Ion Channel.

The journal of physical chemistry. B·2025

Same author

Statistical Molecular Interaction Fields: A Fast and Informative Tool for Characterizing RNA and Protein-Binding Pockets.

Journal of chemical theory and computation·2025

Same author

NOX Transmembrane Electron Transfer Is Governed by a Subtly Balanced, Self-Adjusting Charge Distribution.

Journal of chemical information and modeling·2025

Same author

BioSpring: An elastic network framework for interactive exploration of macromolecular mechanics.

Protein science : a publication of the Protein Society·2025

Search research articles

Related Experiment Video

Updated: Jul 8, 2026

SNARE-mediated Fusion of Single Proteoliposomes with Tethered Supported Bilayers in a Microfluidic Flow Cell Monitored by Polarized TIRF Microscopy

SNARE-mediated Fusion of Single Proteoliposomes with Tethered Supported Bilayers in a Microfluidic Flow Cell Monitored by Polarized TIRF Microscopy

Published on: August 24, 2016

Interactions between neuronal fusion proteins explored by molecular dynamics.

Marie-Pierre Durrieu¹, Richard Lavery, Marc Baaden

¹Institut de Biologie Physico-Chimique, Laboratoire de Biochimie Théorique, Centre National de la Recherche Scientifique, UPR 9080, Paris, France.

Biophysical Journal

|January 24, 2008

Summary

Atomistic simulations reveal the neuronal SNARE complex acts like molecular Velcro, with electrostatic forces dominating interactions. This provides a new framework for understanding mutation impacts on this crucial protein complex.

More Related Videos

A Model Membrane Platform for Reconstituting Mitochondrial Membrane Dynamics

A Model Membrane Platform for Reconstituting Mitochondrial Membrane Dynamics

Published on: September 2, 2020

Cell-cell Fusion of Genome Edited Cell Lines for Perturbation of Cellular Structure and Function

Cell-cell Fusion of Genome Edited Cell Lines for Perturbation of Cellular Structure and Function

Published on: December 7, 2019

Related Experiment Videos

Last Updated: Jul 8, 2026

SNARE-mediated Fusion of Single Proteoliposomes with Tethered Supported Bilayers in a Microfluidic Flow Cell Monitored by Polarized TIRF Microscopy

SNARE-mediated Fusion of Single Proteoliposomes with Tethered Supported Bilayers in a Microfluidic Flow Cell Monitored by Polarized TIRF Microscopy

Published on: August 24, 2016

A Model Membrane Platform for Reconstituting Mitochondrial Membrane Dynamics

A Model Membrane Platform for Reconstituting Mitochondrial Membrane Dynamics

Published on: September 2, 2020

Cell-cell Fusion of Genome Edited Cell Lines for Perturbation of Cellular Structure and Function

Cell-cell Fusion of Genome Edited Cell Lines for Perturbation of Cellular Structure and Function

Published on: December 7, 2019

Area of Science:

Molecular biology
Biophysics
Computational chemistry

Background:

The neuronal SNARE complex mediates membrane fusion, a critical process in neurotransmitter release.
Understanding its structural dynamics and interactions is key to deciphering synaptic transmission.

Purpose of the Study:

To elucidate the structural features and interaction dynamics of the neuronal SNARE complex.
To validate simulation findings against experimental data.

Main Methods:

Atomistic molecular dynamics simulations using AMBER and GROMOS force fields.
Exploration of both explicit and implicit solvent environments.
Analysis of atomic contacts, hydrogen bonds, and salt bridges.

Main Results:

The SNARE core complex exhibits limited conformational dynamics, behaving like a rigid rod.
Electrostatic interactions are dominant, with a characteristic pattern reinforcing the layered structure.
Asymmetric interactions within the four-helix bundle were observed, with R-SNARE being more rigid than Q-SNAREs.
Simulations showed excellent agreement with experimental findings.

Conclusions:

The findings support the 'molecular Velcro' model for the neuronal SNARE complex.
The detailed interaction patterns offer a new tool for interpreting the effects of mutations.
The study provides robust insights into SNARE complex structure and dynamics across different simulation conditions.