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

Membrane Asymmetry Regulating Transporters01:19

Membrane Asymmetry Regulating Transporters

4.4K
Enzymes like flippase, floppase, and scramblase transfer phospholipids from one layer to another in the membrane, thereby affecting membrane asymmetry.
Flippase
Eukaryotic flippases are type-IV P-type ATPases or P4-ATPases belonging to P-type ATPase family proteins that are membrane-bound pumps involved in the ATP-mediated transport of ions and molecules across the membrane. Flippases flip specific phospholipids from the outer to the inner leaflet of a membrane. All P4-ATPases have one...
4.4K
Fluid Mosaic Model01:19

Fluid Mosaic Model

11.6K
Scientists identified the plasma membrane in the 1890s and its principal chemical components (lipids and proteins) by 1915. The model for plasma membrane structure, proposed in 1935 by Hugh Davson and James Danielli, was the first model to be widely accepted in the scientific community. The model was based on the plasma membrane's "railroad track" appearance in early electron micrographs. Davson and Danielli theorized that the plasma membrane's structure resembled a sandwich...
11.6K
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

3.1K
Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
3.1K
Protein Diffusion in the Membrane01:24

Protein Diffusion in the Membrane

4.3K
Proteins show rotational as well as lateral diffusion across the membrane. The lateral diffusion of proteins was confirmed through the cell fusion experiment where mouse and human cells were fused, resulting in hybrid cells. When the human and mouse cells fused, the specific membrane proteins on human and mouse cells were marked with the red and green-fluorescent markers, respectively. Initially, the red and green fluorescence was located on the respective hemisphere of the cell. As time...
4.3K
Single-pass Transmembrane Proteins01:25

Single-pass Transmembrane Proteins

5.0K
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...
5.0K
Multi-pass Transmembrane Proteins and β-barrels01:09

Multi-pass Transmembrane Proteins and β-barrels

5.3K
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...
5.3K

You might also read

Related Articles

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

Sort by
Same author

Fluorogenic Sydnones for Bioorthogonal Labeling of DNA.

Chemistry (Weinheim an der Bergstrasse, Germany)·2026
Same author

Cystic glioblastoma is associated with alterations of KDR and the Rb pathway: a single-center retrospective analysis.

Acta neuropathologica communications·2026
Same author

Uncovering Aggregation-Induced Emission in Carbon Dots for Color-Changing Hydrogels and Information Encryption.

Angewandte Chemie (International ed. in English)·2026
Same author

Understanding Wavelength-Dependent Photopolymerizations via Nano-Second Resolved Transient Spectroscopy.

Journal of the American Chemical Society·2026
Same author

BRAF<sup>V600E</sup> patient derived colon cancer organoids identify biomarkers of response to EGFR and BRAF inhibition and replicate clinical data.

Journal of experimental & clinical cancer research : CR·2026
Same author

A solid-phase click<sup>2</sup> strategy for chromophore-DNA conjugates and their application as a light harvesting system.

Chemical communications (Cambridge, England)·2026

Related Experiment Video

Updated: Jun 21, 2025

Fluorescent Leakage Assay to Investigate Membrane Destabilization by Cell-Penetrating Peptide
07:33

Fluorescent Leakage Assay to Investigate Membrane Destabilization by Cell-Penetrating Peptide

Published on: December 19, 2020

6.3K

Flavin-induced charge separation in transmembrane model peptides.

Samantha Wörner1, Pascal Rauthe2, Johannes Werner2

  • 1Karlsruhe Institute of Technology (KIT), Institute of Organic Chemistry, Fritz-Haber-Weg 6, 76131 Karlsruhe, Germany. Wagenknecht@kit.edu.

Organic & Biomolecular Chemistry
|July 8, 2024
PubMed
Summary
This summary is machine-generated.

Researchers created modified helical peptides that mimic natural biological processes. These peptides demonstrate photo-induced charge transport across membranes, offering insights into photosynthesis and electron transfer.

More Related Videos

Measuring Peptide Translocation into Large Unilamellar Vesicles
12:27

Measuring Peptide Translocation into Large Unilamellar Vesicles

Published on: January 27, 2012

13.8K
A Fluorescence-based Assay of Phospholipid Scramblase Activity
09:52

A Fluorescence-based Assay of Phospholipid Scramblase Activity

Published on: September 20, 2016

13.9K

Related Experiment Videos

Last Updated: Jun 21, 2025

Fluorescent Leakage Assay to Investigate Membrane Destabilization by Cell-Penetrating Peptide
07:33

Fluorescent Leakage Assay to Investigate Membrane Destabilization by Cell-Penetrating Peptide

Published on: December 19, 2020

6.3K
Measuring Peptide Translocation into Large Unilamellar Vesicles
12:27

Measuring Peptide Translocation into Large Unilamellar Vesicles

Published on: January 27, 2012

13.8K
A Fluorescence-based Assay of Phospholipid Scramblase Activity
09:52

A Fluorescence-based Assay of Phospholipid Scramblase Activity

Published on: September 20, 2016

13.9K

Area of Science:

  • Biochemistry
  • Biophysics
  • Molecular Biology

Background:

  • The epidermal growth factor receptor contains an alpha-helical transmembrane segment crucial for cellular signaling.
  • Understanding transmembrane charge transport is key to elucidating biological energy conversion processes like photosynthesis.

Purpose of the Study:

  • To create and characterize synthetic peptide models of alpha-helical transmembrane segments.
  • To investigate the photo-induced transmembrane charge transport capabilities of these modified peptides.
  • To explore the role of specific amino acid residues in initiating and propagating charge transfer.

Main Methods:

  • Synthetic modification of hydrophobic peptides with flavin (photo-inducible charge donor) and tryptophan (charge acceptor) residues.
  • Spectroscopic analysis, including steady-state and time-resolved optical spectroscopy, to examine charge transport.
  • Incorporation of peptides into lipid vesicles and multibilayers to study behavior in membrane-mimetic environments.

Main Results:

  • Modified peptides maintained their helical conformation in various environments, including lipid bilayers.
  • Photo-induced charge transport across the membrane was successfully demonstrated.
  • The tryptophan residue nearest the flavin donor was identified as critical for initiating charge transport at the N-terminus.
  • Subsequent tryptophan residues appear to facilitate charge propagation along the transmembrane helix.

Conclusions:

  • Artificially modified helical peptides serve as valuable models for studying transmembrane electron transfer.
  • These models provide insights into the fundamental principles governing charge transport in biological systems, including photosynthesis.
  • The synthetic design allows for controlled investigation of electron transfer mechanisms in membrane proteins.