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

Mechanisms of Membrane-bending01:15

Mechanisms of Membrane-bending

The living membranes are flexible due to their fluid mosaic nature; however, their bending into different shapes is an active process regulated by specific lipids and proteins. The membrane bending can be transient as seen in vesicles or stable for a long time as in microvilli. Cells regulate the size, location, and duration of the membrane curvature.
Membrane bending can happen due to intrinsic changes in lipid composition or extrinsic association with different proteins. The proteins involved...
Multi-pass Transmembrane Proteins and β-barrels01:09

Multi-pass Transmembrane Proteins and β-barrels

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 G-protein-linked receptors (GPCRs) and...
Protein Folding01:22

Protein Folding

Overview
Protein Folding01:25

Protein Folding

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...
Mechanisms of Membrane Domain Formation00:59

Mechanisms of Membrane Domain Formation

Different physical properties of lipids and proteins allow them to localize and form distinct islands or domains in the membrane. Some membrane domains are formed due to protein-protein interactions, whereas others are formed due to the presence of specific lipids such as sphingolipids and sterols—for example, large proteins, such as bacteriorhodopsin, aggregate and create distinct domains.
Another mechanism for membrane domain formation involves membrane proteins interacting with cytoskeletal...
Amyloid Fibrils03:03

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...

You might also read

Related Articles

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

Sort by
Same author

Retraction Note: Mechanism of HCV's resistance to IFN-α in cell culture involves expression of functional IFN-α receptor 1.

Virology journal·2026
Same author

Evaluation of stored whole blood cellular components treated with bactericidal peptides at a higher concentration than required to assess the peptide compatibility with product quality.

Blood transfusion = Trasfusione del sangue·2026
Same author

pH-Responsive peptide nanopores are stabilized by lipid and water-mediated hydrogen bonding networks.

Nanoscale·2026
Same author

An outer membrane vesicle vaccine prevents lung pathology in a macaque model of pneumonic melioidosis.

Nature communications·2025
Same author

Antimicrobial Peptides Can Facilitate Whole Blood Safety from Bacteria: A Proof of Concept.

ACS infectious diseases·2025
Same author

Anion-Facilitated Hydrogen-Deuterium Exchange as a Tool to Probe Weak Anion-Protein Interactions Responsible for Hofmeister Effects.

The journal of physical chemistry. B·2025
Same journal

Tau protein differentially affects Piezo1 and Kir2.1 channels in brain capillary endothelial cells.

Biophysical journal·2026
Same journal

Emergent Intercellular Junction Stability during Cyclic Tissue Loading.

Biophysical journal·2026
Same journal

Enhanced-Sampling Simulations Reveal Distinct Intermediates in SARS-CoV-2 FSE Pseudoknot Interconversion.

Biophysical journal·2026
Same journal

Structure-based simulations of the full Flock House virus capsid reveal pathways and energetics of an infection-critical peptide externalization event.

Biophysical journal·2026
Same journal

Quantifying the Peripheral Surface Information Entropy from Conformational Ensembles of Globular Protein-Peptide Complexes.

Biophysical journal·2026
Same journal

Anisotropic unbinding and location-dependent hovering of a kinesin motor head over microtubule.

Biophysical journal·2026
See all related articles

Related Experiment Video

Updated: May 30, 2026

Reconstitution of Septin Assembly at Membranes to Study Biophysical Properties and Functions
06:32

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

Published on: July 28, 2022

Structural plasticity in self-assembling transmembrane β-sheets.

Christopher M Bishop1, William C Wimley

  • 1Department of Biochemistry, Tulane University School of Medicine, New Orleans, Louisiana, USA.

Biophysical Journal
|August 17, 2011
PubMed
Summary
This summary is machine-generated.

Membrane-spanning beta-sheets show remarkable structural plasticity. These AcWL(n) peptides form stable structures in lipid bilayers, adapting to different membrane thicknesses and phases.

More Related Videos

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
06:45

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay

Published on: May 26, 2011

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
07:26

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Published on: November 21, 2013

Related Experiment Videos

Last Updated: May 30, 2026

Reconstitution of Septin Assembly at Membranes to Study Biophysical Properties and Functions
06:32

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

Published on: July 28, 2022

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
06:45

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay

Published on: May 26, 2011

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
07:26

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Published on: November 21, 2013

Area of Science:

  • Biophysics
  • Membrane Biology
  • Protein Structure

Background:

  • Membrane proteins often adopt beta-sheet structures.
  • The structural flexibility of transmembrane beta-sheets is not fully understood.
  • Understanding peptide-lipid interactions is crucial for membrane biophysics.

Purpose of the Study:

  • To investigate the structural plasticity of membrane-spanning beta-sheets.
  • To determine how peptide length and bilayer thickness affect beta-sheet structure.
  • To examine the impact of beta-sheet peptides on lipid bilayer phases.

Main Methods:

  • Incorporation of AcWL(n) peptides (n=5, 6, 7) into phosphatidylcholine lipid bilayers.
  • Differential scanning calorimetry (DSC) to study phase transitions.
  • Circular dichroism (CD) spectroscopy to analyze secondary structure.

Main Results:

  • AcWL(n) peptides form stable, peptide-rich gel phases in lipid bilayers.
  • These beta-sheets are non-membrane-disrupting across various lipid compositions and thicknesses.
  • Incorporation of up to 20 mol% peptide resulted in gel phases with melting temperatures similar to or higher than pure lipid bilayers.

Conclusions:

  • The AcWL(n) family of membrane-inserted beta-sheets demonstrates significant structural plasticity.
  • These peptides adapt to varying membrane environments without compromising bilayer integrity.
  • The findings contribute to understanding the dynamic nature of beta-sheet proteins within lipid membranes.