Jove
Visualize
Contact Us

Related Concept Videos

Multi-pass Transmembrane Proteins and β-barrels01:09

Multi-pass Transmembrane Proteins and β-barrels

6.7K
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...
6.7K
Protein Folding01:25

Protein Folding

11.9K
Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
11.9K
Protein Folding01:22

Protein Folding

128.9K
Overview
128.9K
Single-pass Transmembrane Proteins01:25

Single-pass Transmembrane Proteins

6.9K
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...
6.9K
Introduction to Membrane Proteins01:16

Introduction to Membrane Proteins

82.3K
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...
82.3K
Insertion of Multi-pass Transmembrane Proteins in the RER01:29

Insertion of Multi-pass Transmembrane Proteins in the RER

19.0K
The rough ER membrane synthesizes, assembles, and embeds transmembrane proteins in diverse topologies. These proteins function as transporters or channels and can remain in the ER membrane or are sent to the Golgi complex, lysosome, and cell membrane.
The multipass transmembrane proteins are the type IV integral membrane proteins with multiple topogenic sequences determining their spatial arrangement in the ER membrane. Nearly all multipass proteins lack a cleavable signal sequence and use...
19.0K

You might also read

Related Articles

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

Sort by
Same author

Kindlin-3 sustains cytokine interleukin-2 signaling by linking its receptor to integrin LFA-1.

The Journal of biological chemistry·2026
Same author

The interaction of XPG with TFIIH through p62 and XPD is required for the completion of nucleotide excision repair.

Nucleic acids research·2026
Same author

Design and characterization of calprotectin tetramerization variants for probing the role of oligomerization in receptor activation.

Protein science : a publication of the Protein Society·2025
Same author

Structures, Interactions, and Antimicrobial Activity of the Shortest Thanatin Peptide from <i>Anasa tristis</i>.

International journal of molecular sciences·2025
Same author

A new multisystem ERCC1-hepatorenal syndrome: insights from a clinical cohort, molecular pathogenesis, and management guidelines.

European journal of human genetics : EJHG·2025
Same author

Single Disulfide Bond in Host Defense Thanatin Analog Peptides: Antimicrobial Activity, Atomic-Resolution Structures and Target Interactions.

International journal of molecular sciences·2025
Same journal

Enhanced and selective oxygen reduction by iron porphyrin with a biguanide residue in the second coordination sphere.

Chemical science·2026
Same journal

Excited-state orbital angular momentum enables all-optical molecular spin coherence.

Chemical science·2026
Same journal

Polyvinyl-based hole-transporting materials processed with non-destructive and green solvents for tin-lead perovskite solar cells and all-perovskite tandems.

Chemical science·2026
Same journal

Pd-catalyzed regio- and enantioselective allylation of cyclic allylboronates.

Chemical science·2026
Same journal

Covalent polyoxometalate-polyimide hybridization: multi-scale molecular engineering toward high-performance sodium-ion battery anodes.

Chemical science·2026
Same journal

Catalytic visible light-driven alkane dehydrogenation by a di-uranyl germanotungstate.

Chemical science·2026
See all related articles
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 Experiment Video

Updated: Feb 27, 2026

Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation
11:09

Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation

Published on: August 1, 2018

11.3K

Designed multi-stranded heme binding β-sheet peptides in membrane.

Areetha D'Souza1, Mukesh Mahajan1, Surajit Bhattacharjya1

  • 1School of Biological Sciences , 60 Nanyang Drive , 637551 , Singapore .

Chemical Science
|June 30, 2017
PubMed
Summary
This summary is machine-generated.

Scientists designed novel membrane-soluble beta-sheet peptides that bind heme, enabling new protein engineering for membrane functions like electron transfer and enzymatic activity.

More Related Videos

Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies
12:05

Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies

Published on: March 6, 2013

14.7K
Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules
10:58

Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules

Published on: July 25, 2013

17.7K

Related Experiment Videos

Last Updated: Feb 27, 2026

Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation
11:09

Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation

Published on: August 1, 2018

11.3K
Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies
12:05

Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies

Published on: March 6, 2013

14.7K
Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules
10:58

Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules

Published on: July 25, 2013

17.7K

Area of Science:

  • Protein Engineering and Design
  • Biophysical Chemistry
  • Membrane Biology

Background:

  • Designed peptides with defined structures are crucial for membrane-associated biological processes.
  • Heme proteins are versatile, inspiring designs for helical peptides; however, designed beta-sheet heme proteins are underexplored due to folding complexities.
  • Naturally occurring beta-sheet proteins can be membrane-soluble and bind heme, indicating potential for designed analogs.

Purpose of the Study:

  • To design and characterize novel membrane-soluble beta-sheet peptides capable of binding heme and di-heme.
  • To investigate the structural basis and functional capabilities of these designed peptides in a membrane environment.
  • To explore the potential of beta-sheet protein design for new applications in biocatalysis and energy conversion.

Main Methods:

  • Design of four- and six-stranded beta-sheet peptides incorporating D-amino acid residues for beta-turn nucleation.
  • Utilized bis-His coordination between antiparallel beta-strands for heme ligation.
  • Employed beta- and omega-amino acids to optimize high-affinity heme binding pockets (nanomolar dissociation constants).

Main Results:

  • Successfully designed and structurally characterized membrane-soluble beta-sheet peptides binding heme and di-heme.
  • Demonstrated increasing heme binding affinity with omega-amino acid alkyl chain length, achieving nanomolar affinity.
  • Observed cooperative di-heme binding in a six-stranded peptide and functional peroxidase activity and electron transfer with cytochrome c.

Conclusions:

  • This study presents the first designed functional beta-sheet proteins in a membrane environment.
  • The developed peptides expand the toolkit for creating novel heme proteins with tailored functions.
  • The findings pave the way for engineering membrane-active proteins for diverse biotechnological applications.