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

Molecular Shapes01:18

Molecular Shapes

Molecules have characteristic shapes that are crucial for their function. The arrangement of various electron groups around the central atom dictates their molecular geometry. Electron pairs in the valence shell of a central atom will adopt an arrangement that minimizes repulsions between the electron pairs by maximizing the distance between them. The valence electrons form either bonding pairs, located primarily between bonded atoms, or lone pairs.
Two regions of electron density in a diatomic...
Molecular Models02:00

Molecular Models

Physical models representing molecular architectures of chemical compounds play essential roles in understanding chemistry. The use of molecular models makes it easier to visualize the structures and shapes of atoms and molecules.
Molecular Shape and Polarity03:37

Molecular Shape and Polarity

Dipole Moment of a Molecule
VSEPR Theory and the Basic Shapes02:52

VSEPR Theory and the Basic Shapes

Overview of VSEPR Theory
VSEPR Theory02:37

VSEPR Theory

Valence shell electron-pair repulsion theory (VSEPR theory) enables us to predict the molecular structure around a central atom from an examination of the number of bonds and lone electron pairs in its Lewis structure. The VSEPR model assumes that electron pairs in the valence shell of a central atom will adopt an arrangement that minimizes repulsions between these electron pairs by maximizing the distance between them. The electrons in the valence shell of a central atom form either bonding...
Predicting Molecular Geometry02:27

Predicting Molecular Geometry

VSEPR Theory for Determination of Electron Pair Geometries

You might also read

Related Articles

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

Sort by
Same author

Structures of asymmetric particles of tick-borne encephalitis virus provide insight into flavivirus assembly and maturation.

Science advances·2026
Same author

Implicit membrane for helical peptide selectivity toward bacterial membranes.

Biophysical journal·2026
Same author

Nucleation Kinetics Reveals a Distinct Biological Function Space of Biomolecular Condensates.

Advanced science (Weinheim, Baden-Wurttemberg, Germany)·2026
Same author

Correction to "Martini 3 Limitations in Phospholipid Flip-Flop".

Journal of chemical theory and computation·2026
Same author

The second Gibbs paradox.

The Journal of chemical physics·2026
Same author

Monte Carlo methods, 70 years after "Equation of state calculations by fast computing machines" by Nicholas Metropolis, Arianna Rosenbluth, Marshall Rosenbluth, Augusta Teller, and Edward Teller (1953).

The Journal of chemical physics·2025

Related Experiment Video

Updated: May 29, 2026

Controlling the Size, Shape and Stability of Supramolecular Polymers in Water
16:24

Controlling the Size, Shape and Stability of Supramolecular Polymers in Water

Published on: August 2, 2012

Relation between molecular shape and the morphology of self-assembling aggregates: a simulation study.

Robert Vácha1, Daan Frenkel

  • 1Department of Chemistry, University of Cambridge, Cambridge, United Kingdom. rv260@cam.ac.uk

Biophysical Journal
|September 28, 2011
PubMed
Summary

Protein aggregation simulations reveal how particle shape and interactions dictate aggregate structures like ribbons and fibrils. Model parameters, including stripe width and end interactions, control protein aggregate morphology.

More Related Videos

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

Self-assembling Morphologies Obtained from Helical Polycarbodiimide Copolymers and Their Triazole Derivatives
09:22

Self-assembling Morphologies Obtained from Helical Polycarbodiimide Copolymers and Their Triazole Derivatives

Published on: February 7, 2017

Related Experiment Videos

Last Updated: May 29, 2026

Controlling the Size, Shape and Stability of Supramolecular Polymers in Water
16:24

Controlling the Size, Shape and Stability of Supramolecular Polymers in Water

Published on: August 2, 2012

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

Self-assembling Morphologies Obtained from Helical Polycarbodiimide Copolymers and Their Triazole Derivatives
09:22

Self-assembling Morphologies Obtained from Helical Polycarbodiimide Copolymers and Their Triazole Derivatives

Published on: February 7, 2017

Area of Science:

  • Biophysics
  • Computational Biology
  • Materials Science

Background:

  • Proteins can form diverse aggregate structures, both compact and extended.
  • Understanding these structures is crucial for various biological and material applications.

Purpose of the Study:

  • To simulate protein aggregation using a coarse-grained anisotropic model.
  • To identify key parameters governing protein aggregate morphology.
  • To establish a link between protein-protein interaction potentials and aggregate structures.

Main Methods:

  • Coarse-grained anisotropic modeling of rodlike particles.
  • Monte Carlo simulations to explore parameter space.
  • Analysis of aggregate morphologies, including ribbons, fibrils, and vesicles.

Main Results:

  • The model successfully reproduces experimentally observed protein aggregate structures.
  • All simulated structures have corresponding experimental counterparts.
  • Aggregate morphology is critically dependent on the width of an attractive stripe and end interactions.
  • Simulations reveal a generic relationship between interaction potential shape and aggregate morphology.

Conclusions:

  • The study provides a generic insight into protein aggregation mechanisms.
  • The findings offer a framework for predicting and controlling protein aggregate structures.
  • The model serves as a valuable tool for understanding protein self-assembly.