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%...

You might also read

Related Articles

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

Sort by

Same author

Cadmium-induced structural reorganization and coordination evolution in SeTeSn chalcogenide glasses: correlation with photon interaction behaviour.

RSC advances·2026

Same author

Pump-probe X-ray holographic imaging of laser-induced cavitation bubbles with femtosecond FEL pulses.

Nature communications·2021

Same author

Iterative micro-tomography of biopsy samples from truncated projections with quantitative gray values.

Physics in medicine and biology·2021

Same author

Spectral µCT with an energy resolving and interpolating pixel detector.

Optics express·2020

Same author

Correlative microscopy approach for biology using X-ray holography, X-ray scanning diffraction and STED microscopy.

Nature communications·2018

Same author

Publisher Correction: Four dimensional material movies: High speed phase-contrast tomography by backprojection along dynamically curved paths.

Scientific reports·2018

Search research articles

Related Experiment Video

Updated: Dec 24, 2025

Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae

Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae

Published on: January 10, 2018

SARS E protein in phospholipid bilayers: an anomalous X-ray reflectivity study.

Z Khattari¹, G Brotons¹, E Arbely²

¹Institut für Röntgenphysik, Universität Göttingen, Geiststrasse 11, 37073 Göttingen, Germany.

Physica. B, Condensed Matter

|April 15, 2020

Summary

Anomalous X-ray reflectivity precisely located an iodine-labelled phenylalanine within the SARS E protein embedded in a lipid bilayer. This method provides crucial data on protein conformation within cell membranes.

Keywords:

Anomalous scattering Lipid-peptide interaction SARS E protein

More Related Videos

A Nanobar-Supported Lipid Bilayer System for the Study of Membrane Curvature Sensing Proteins in vitro

A Nanobar-Supported Lipid Bilayer System for the Study of Membrane Curvature Sensing Proteins in vitro

Published on: November 30, 2022

Reconstitution of Septin Assembly at Membranes to Study Biophysical Properties and Functions

Reconstitution of Septin Assembly at Membranes to Study Biophysical Properties and Functions

Published on: July 28, 2022

Related Experiment Videos

Last Updated: Dec 24, 2025

Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae

Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae

Published on: January 10, 2018

A Nanobar-Supported Lipid Bilayer System for the Study of Membrane Curvature Sensing Proteins in vitro

A Nanobar-Supported Lipid Bilayer System for the Study of Membrane Curvature Sensing Proteins in vitro

Published on: November 30, 2022

Reconstitution of Septin Assembly at Membranes to Study Biophysical Properties and Functions

Reconstitution of Septin Assembly at Membranes to Study Biophysical Properties and Functions

Published on: July 28, 2022

Area of Science:

Structural Biology
Biophysics
Membrane Protein Research

Background:

Understanding membrane protein conformation is vital for drug development and cellular function.
X-ray reflectivity is a powerful technique for studying interfaces and thin films.
Previous studies have explored protein localization within lipid bilayers.

Purpose of the Study:

To determine the precise location of an iodine-labelled phenylalanine residue in the SARS E protein.
To investigate the conformational constraints of membrane proteins within a lipid bilayer environment.
To assess the utility of anomalous X-ray reflectivity for residue-specific localization.

Main Methods:

Anomalous X-ray reflectivity experiments were performed on multilamellar stacks of DMPC phospholipid bilayers.
An iodine-labelled phenylalanine residue was incorporated into the SARS E protein.
Data analysis involved Fourier synthesis to obtain the electron density profile.

Main Results:

The study successfully demonstrated the feasibility of locating a specific labelled residue within a membrane protein.
Electron density profiles were generated, providing insights into the protein's position relative to the lipid bilayer.
Challenges in Fourier synthesis analysis for complex membrane systems were identified.

Conclusions:

Anomalous X-ray reflectivity is a viable technique for high-resolution structural analysis of membrane proteins.
The findings contribute to a better understanding of SARS E protein structure and its interaction with lipid bilayers.
This approach can be extended to study other membrane proteins and their conformational states.