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

Introduction to Membrane Proteins01:16

Introduction to Membrane Proteins

81.1K
The cell membrane, or plasma membrane, is an ever-changing landscape. It is described as a fluid mosaic where various macromolecules are embedded in the phospholipid bilayer. Among the macromolecules are proteins. The protein content varies across cell types. For example, mitochondrial inner membranes contain ~76% protein content, while myelin contains ~18% protein content. Individual cells contain many types of membrane proteins—red blood cells contain over 50—and different cell...
81.1K
Assembly of the Lipid Bilayer in the ER01:28

Assembly of the Lipid Bilayer in the ER

4.2K
Biological membranes are more than just a barrier separating cell cytoplasm from the outside environment. They are highly dynamic and help maintain the integrity and physiological stability of the cells as well as membrane-bound organelles. Membranes also play vital roles in cell-to-cell and intracellular communication.
A large chunk of any biological membrane is composed of phospholipids. These lipids have a heterogeneous distribution across different subcellular organelles and even between...
4.2K
Asymmetric Lipid Bilayer01:35

Asymmetric Lipid Bilayer

9.9K
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%...
9.9K
Membrane Lipids01:32

Membrane Lipids

34.2K
Lipids are an essential component of all biological membranes. The average lipid content in mammalian membranes is 50%, though it can be as low as 20% in the inner mitochondrial membrane or as high as 80% in the myelin sheath present around the nerve cells.
Phosphatidylcholine, phosphatidylethanolamine, phosphatidylserine, and sphingomyelin are the most common phospholipids present in mammalian membranes. At physiological pH, phosphatidylserine is negatively charged, while the other three...
34.2K
What are Lipids?01:38

What are Lipids?

220.4K
Overview
220.4K
Porin Insertion in the Outer Mitochondrial Membrane01:12

Porin Insertion in the Outer Mitochondrial Membrane

4.8K
Porins are beta-barrel proteins translocated to the mitochondrial outer membrane through the TOM complex into the intermembrane space. Porin precursors bind TIM chaperones within the intermembrane space and are guided to the Sorting and Assembly Machinery complex or SAM complex on the outer mitochondrial membrane.
Three models describe the assembly of porins by the SAM complex and their insertion into the outer membrane. Model 1 suggests that porins are assembled outside the SAM channel as the...
4.8K

You might also read

Related Articles

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

Sort by
Same author

Mapping mRNA Localization and Internal Structure in Lipid Nanoparticles through Solid-State Dynamic Nuclear Polarization NMR and Proton Spin-Diffusion Modeling.

Small methods·2026
Same author

Investigation of the Interactions and pH-Dependent Structural Changes in Helical Peptides by Molecular Dynamics Simulations.

The journal of physical chemistry. B·2026
Same author

Overcoming the barriers to the scaled-up production of therapeutic bacterial extracellular vesicles.

Nanomedicine (London, England)·2026
Same author

Mixture dependent correlation patterns in antibacterial and cytotoxic activities of five hop isolates.

Scientific reports·2026
Same author

Is faster always better? A critical assessment of Vibrio natriegens as microbial host for recombinant protein production.

Bioprocess and biosystems engineering·2026
Same author

Electronic Structures of Pt(0) Complexes and Atomically Precise Clusters from Solid-State <sup>195</sup>Pt NMR Signatures.

Journal of the American Chemical Society·2026

Related Experiment Video

Updated: Feb 2, 2026

A Nanobar-Supported Lipid Bilayer System for the Study of Membrane Curvature Sensing Proteins in vitro
08:27

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

Published on: November 30, 2022

3.4K

Probing Membrane Protein Insertion into Lipid Bilayers by Solid-State NMR.

Eszter E Najbauer1, Kumar Tekwani Movellan1, Tobias Schubeis2

  • 1Department of NMR based Structural Biology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077, Göttingen, Germany.

Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry
|November 20, 2018
PubMed
Summary
This summary is machine-generated.

Proton-detected solid-state NMR reveals site-specific protein environments. This method efficiently measures exposure to water and lipids, aiding in understanding protein function and structure.

Keywords:
lipid bilayermagic-angle spinningmembrane proteinsolid-state NMRsurface environment

More Related Videos

Automated Lipid Bilayer Membrane Formation Using a Polydimethylsiloxane Thin Film
08:23

Automated Lipid Bilayer Membrane Formation Using a Polydimethylsiloxane Thin Film

Published on: July 10, 2016

19.1K
Detergent-free Ultrafast Reconstitution of Membrane Proteins into Lipid Bilayers Using Fusogenic Complementary-charged Proteoliposomes.
11:10

Detergent-free Ultrafast Reconstitution of Membrane Proteins into Lipid Bilayers Using Fusogenic Complementary-charged Proteoliposomes.

Published on: April 5, 2018

11.7K

Related Experiment Videos

Last Updated: Feb 2, 2026

A Nanobar-Supported Lipid Bilayer System for the Study of Membrane Curvature Sensing Proteins in vitro
08:27

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

Published on: November 30, 2022

3.4K
Automated Lipid Bilayer Membrane Formation Using a Polydimethylsiloxane Thin Film
08:23

Automated Lipid Bilayer Membrane Formation Using a Polydimethylsiloxane Thin Film

Published on: July 10, 2016

19.1K
Detergent-free Ultrafast Reconstitution of Membrane Proteins into Lipid Bilayers Using Fusogenic Complementary-charged Proteoliposomes.
11:10

Detergent-free Ultrafast Reconstitution of Membrane Proteins into Lipid Bilayers Using Fusogenic Complementary-charged Proteoliposomes.

Published on: April 5, 2018

11.7K

Area of Science:

  • Biophysics
  • Structural Biology
  • Biochemistry

Background:

  • Understanding a protein's environment is crucial for deciphering its function and inferring structural properties.
  • Membrane proteins, like the human voltage-dependent anion channel and alkane transporter AlkL, play vital roles in cellular processes.

Purpose of the Study:

  • To develop and demonstrate a method for site-specific determination of the protein environment using solid-state NMR.
  • To investigate the interaction of membrane proteins with mobile water and lipids.

Main Methods:

  • Utilized proton-detected solid-state NMR spectroscopy.
  • Employed conditions of fast magic-angle spinning, high magnetic field, and sample deuteration to reduce spin diffusion.
  • Applied the technique to two model membrane proteins: human voltage-dependent anion channel and Pseudomonas putida alkane transporter AlkL.

Main Results:

  • Demonstrated efficient measurement of site-specific exposure to mobile water and lipids.
  • Observed selective lipid transfer in the membrane-spanning regions of the studied proteins.
  • Determined an average lipid-protein transfer rate of 6 s-1 for protected residues and intra-protein transfer rates of 8-15 s-1.

Conclusions:

  • The developed solid-state NMR approach enables precise characterization of protein-lipid and protein-water interactions.
  • The findings provide insights into the structural dynamics and functional mechanisms of membrane proteins.
  • Site-specific environmental information aids in understanding protein structure-function relationships.