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

Protein Folding01:22

Protein Folding

128.2K
Overview
128.2K
Protein Folding01:25

Protein Folding

11.6K
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...
11.6K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

19.9K
The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
19.9K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

15.1K
15.1K
Peptide Bonds02:43

Peptide Bonds

83.5K
A peptide bond covalently attaches amino acids through a dehydration reaction. One amino acid's carboxyl group and another amino acid's amino group combine, releasing a water molecule. The resulting bond is the peptide bond. The products that such linkages form are peptides. As more amino acids join this growing chain, the resulting chain is a polypeptide. Each polypeptide has a free amino group at one end. This end has the N-terminal, or the amino-terminal, and the other end has a free...
83.5K
C4 Pathway and CAM01:27

C4 Pathway and CAM

49.3K
Most plants use the C3 pathway for carbon fixation. However, some plants, such as sugar cane, corn, and cacti that grow in hot conditions, use alternative pathways to fix carbon and conserve energy loss due to photorespiration. Photorespiration is the process that occurs when the oxygen concentration is high. Under such conditions, the rubisco enzyme in the Calvin cycle binds O2 instead of CO2, which halts photosynthesis and consumes energy.
C4 Pathway
The C4 pathway is used by plants such as...
49.3K

You might also read

Related Articles

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

Sort by
Same author

Computational Hydropathy Analysis of BamA Bacterial Outer Membrane Protein and Its Mutants.

The journal of physical chemistry. B·2025
Same author

Dimerization Promotes PKR Activation by Modulating Energetics of αC Helix Conversion between Active and Inactive Conformations.

The journal of physical chemistry. B·2024
Same author

The <i>α</i> C helix is a central regulator of PKR activation.

bioRxiv : the preprint server for biology·2024
Same author

Curvature sensing lipid dynamics in a mitochondrial inner membrane model.

Communications biology·2024
Same author

Expanded ensemble predictions of absolute binding free energies in the SAMPL9 host-guest challenge.

Physical chemistry chemical physics : PCCP·2023
Same author

Combined Computational-Biochemical Approach Offers an Accelerated Path to Membrane Protein Solubilization.

Journal of chemical information and modeling·2023

Related Experiment Video

Updated: Feb 12, 2026

Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy
10:09

Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy

Published on: April 28, 2011

18.8K

Folding a viral peptide in different membrane environments: pathway and sampling analyses.

Shivangi Nangia1, Jason G Pattis1, Eric R May2

  • 1Department of Molecular and Cell Biology, University of Connecticut, Storrs, CT, 06269, USA.

Journal of Biological Physics
|April 13, 2018
PubMed
Summary

Flock House virus (FHV) γ peptide disrupts endosomal membranes. Molecular dynamics simulations reveal how this peptide folds into a helical state within different lipid membrane compositions, aiding viral infection studies.

Keywords:
Flock House virusMembrane active peptidesMolecular dynamicsNon-enveloped virusProtein foldingTICAUmbrella sampling

More Related Videos

Preparation of the Rat Vocal Fold for Neuromuscular Analyses
07:17

Preparation of the Rat Vocal Fold for Neuromuscular Analyses

Published on: May 15, 2020

4.0K
A Pathway Association Study Tool for GWAS Analyses of Metabolic Pathway Information
05:01

A Pathway Association Study Tool for GWAS Analyses of Metabolic Pathway Information

Published on: July 1, 2020

3.8K

Related Experiment Videos

Last Updated: Feb 12, 2026

Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy
10:09

Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy

Published on: April 28, 2011

18.8K
Preparation of the Rat Vocal Fold for Neuromuscular Analyses
07:17

Preparation of the Rat Vocal Fold for Neuromuscular Analyses

Published on: May 15, 2020

4.0K
A Pathway Association Study Tool for GWAS Analyses of Metabolic Pathway Information
05:01

A Pathway Association Study Tool for GWAS Analyses of Metabolic Pathway Information

Published on: July 1, 2020

3.8K

Area of Science:

  • Virology
  • Biophysics
  • Computational Biology

Background:

  • Flock House virus (FHV) serves as a model for non-enveloped virus infection mechanisms.
  • Endosomal membrane disruption by the FHV capsid's γ peptide is crucial for viral entry.
  • Understanding peptide-membrane interactions is key to deciphering viral infection pathways.

Purpose of the Study:

  • To investigate the folding mechanism of the FHV γ peptide in various membrane environments.
  • To analyze the influence of membrane composition (neutral vs. anionic lipids) on peptide folding.
  • To elucidate the energetics and configurational dynamics of peptide-membrane interactions.

Main Methods:

  • All-atom molecular dynamics simulations of the FHV γ peptide (21 N-terminal residues).
  • Umbrella sampling calculations to study peptide folding in homogenous and heterogeneous lipid membranes.
  • Analysis of trajectory data for folding energetics and configurational sampling using time-lagged independent component analysis.

Main Results:

  • The FHV γ peptide undergoes folding into a helical state within simulated membranes.
  • Membrane composition significantly impacts the peptide's folding energetics and mechanism.
  • Distinct folding pathways were observed in neutral and anionic lipid environments.

Conclusions:

  • The study provides atomic-level insights into FHV γ peptide's membrane interaction and folding.
  • Findings highlight the role of membrane composition in modulating viral peptide activity.
  • This research contributes to understanding virus-host membrane interactions and developing antiviral strategies.