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 Organization01:24

Protein Organization

10.2K
Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence....
10.2K
Protein Networks02:26

Protein Networks

4.7K
An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
4.7K
Protein-protein Interfaces02:04

Protein-protein Interfaces

15.1K
Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
15.1K
Amyloid Fibrils03:03

Amyloid Fibrils

13.2K
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,...
13.2K
Protein Folding01:22

Protein Folding

131.4K
Overview
131.4K

You might also read

Related Articles

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

Sort by
Same author

Context-Aware Hydrophobicity Modeling: HydroMap and FastHydroMap.

bioRxiv : the preprint server for biology·2026
Same author

Disentangling Intrachain Folding from Interchain Assembly through Multidimensional Visualization.

The journal of physical chemistry. B·2026
Same author

Good Practices for Simulation Studies Published in <i>The Journal of Physical Chemistry B</i>.

The journal of physical chemistry. B·2026
Same author

The Seasons of a Career in Physical Chemistry.

ACS physical chemistry Au·2026
Same author

The Seasons of a Career in Physical Chemistry: Olivia Harper Wilkins.

ACS physical chemistry Au·2026
Same author

The Seasons of a Career in Physical Chemistry: Rajarshi Chakrabarti.

The journal of physical chemistry. B·2026

Related Experiment Video

Updated: Apr 17, 2026

Evaluation of the Impact of Protein Aggregation on Cellular Oxidative Stress in Yeast
11:04

Evaluation of the Impact of Protein Aggregation on Cellular Oxidative Stress in Yeast

Published on: June 23, 2018

7.8K

Computational studies of protein aggregation: methods and applications.

Alex Morriss-Andrews1, Joan-Emma Shea

  • 1Department of Physics and.

Annual Review of Physical Chemistry
|February 5, 2015
PubMed
Summary

This review explores theoretical studies on protein aggregation, focusing on computational models for amyloid fibril formation. Understanding these processes is crucial for diseases like Alzheimer's and functional fibril roles.

Keywords:
amyloid fibrilscoarse-grained modelsenhanced sampling methodsmolecular dynamics simulationsreplica exchange molecular dynamicssystematic coarse graining

More Related Videos

Monitoring Protein Aggregation Kinetics In Vivo using Automated Inclusion Counting in Caenorhabditis elegans
06:49

Monitoring Protein Aggregation Kinetics In Vivo using Automated Inclusion Counting in Caenorhabditis elegans

Published on: December 17, 2021

3.5K
Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy
12:58

Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy

Published on: September 12, 2019

10.4K

Related Experiment Videos

Last Updated: Apr 17, 2026

Evaluation of the Impact of Protein Aggregation on Cellular Oxidative Stress in Yeast
11:04

Evaluation of the Impact of Protein Aggregation on Cellular Oxidative Stress in Yeast

Published on: June 23, 2018

7.8K
Monitoring Protein Aggregation Kinetics In Vivo using Automated Inclusion Counting in Caenorhabditis elegans
06:49

Monitoring Protein Aggregation Kinetics In Vivo using Automated Inclusion Counting in Caenorhabditis elegans

Published on: December 17, 2021

3.5K
Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy
12:58

Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy

Published on: September 12, 2019

10.4K

Area of Science:

  • Biochemistry and Molecular Biology
  • Computational Biology
  • Biophysics

Background:

  • Protein aggregation is the self-assembly of soluble proteins into supramolecular structures.
  • Amyloid fibrils, rich in beta-sheet content, are common end products of protein aggregation.
  • This process is implicated in diseases such as Alzheimer's disease and has functional roles in some organisms.

Purpose of the Study:

  • To review theoretical studies on protein fibril formation.
  • To emphasize computational models and methods used in studying protein aggregation.

Main Methods:

  • Focus on theoretical and computational approaches.
  • Review of common computational models and simulation techniques.
  • Analysis of studies investigating the mechanisms of fibril formation.

Main Results:

  • Theoretical studies provide insights into the complex pathways of protein aggregation.
  • Computational models are essential tools for dissecting the molecular mechanisms of fibril formation.
  • A variety of computational methods are employed to understand the kinetics and thermodynamics of aggregation.

Conclusions:

  • Computational modeling is key to understanding protein aggregation and amyloid fibril formation.
  • Theoretical investigations aid in elucidating disease mechanisms and potential therapeutic targets.
  • Further development of computational methods will enhance our understanding of these critical biological processes.