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

Polymer Classification: Crystallinity01:21

Polymer Classification: Crystallinity

4.3K
Unlike ionic or small covalent molecules, polymers do not form crystalline solids due to the diffusion limitations of their long-chain structures. However, polymers contain microscopic crystalline domains separated by amorphous domains.
Crystalline domains are the regions where polymer chains are aligned in an orderly manner and held together in proximity by intermolecular forces. For example, chains in the crystalline domains of polyethylene and nylon are bound together by van der Waals...
4.3K
Protein and Protein Structure02:15

Protein and Protein Structure

92.3K
Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...
92.3K
Protein Organization01:13

Protein Organization

161.9K
Overview
161.9K
Protein Organization01:24

Protein Organization

10.0K
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....
10.0K
Protein Folding01:22

Protein Folding

130.6K
Overview
130.6K
Protein Folding01:25

Protein Folding

12.5K
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...
12.5K

You might also read

Related Articles

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

Sort by
Same author

Structural insights into allosteric regulation of GdpP: A conformationally dynamic phosphodiesterase.

Structure (London, England : 1993)·2026
Same author

Role of viral protein ratio in the structure and separation of empty and full adeno-associated virus capsids: A molecular dynamics study.

Molecular therapy. Advances·2026
Same author

Two-population Rouse models for polymer segmental dynamics in nanocomposites.

Physical review. E·2026
Same author

Structure of the disulfide-rich modules of a striking tandem repeat protein, avian cysteine-rich eggshell membrane protein.

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

Shear and Dilatational Rheology and Interfacial Structure of a Monoclonal Antibody Adsorbed at the Air-Liquid Interface.

Langmuir : the ACS journal of surfaces and colloids·2025
Same author

Comparative structural and rheological analysis of model and clinical surfactants: role of protein-enriched multilayers and bulk supply.

Soft matter·2025

Related Experiment Video

Updated: Mar 31, 2026

Growing Protein Crystals with Distinct Dimensions Using Automated Crystallization Coupled with In Situ Dynamic Light Scattering
09:15

Growing Protein Crystals with Distinct Dimensions Using Automated Crystallization Coupled with In Situ Dynamic Light Scattering

Published on: August 14, 2018

11.1K

Local Crystalline Structure in an Amorphous Protein Dense Phase.

Daniel G Greene1, Shannon Modla2, Norman J Wagner1

  • 1Department of Chemical and Biomolecular Engineering, University of Delaware, Newark, Delaware.

Biophysical Journal
|October 22, 2015
PubMed
Summary

This study reveals that ovalbumin protein precipitates form core-shell structures. The shell contains nanocrystalline protein networks, challenging the assumption of amorphous protein gels.

More Related Videos

Protein Crystallization for X-ray Crystallography
09:27

Protein Crystallization for X-ray Crystallography

Published on: January 16, 2011

65.9K
Microcrystallography of Protein Crystals and In Cellulo Diffraction
09:35

Microcrystallography of Protein Crystals and In Cellulo Diffraction

Published on: July 21, 2017

9.6K

Related Experiment Videos

Last Updated: Mar 31, 2026

Growing Protein Crystals with Distinct Dimensions Using Automated Crystallization Coupled with In Situ Dynamic Light Scattering
09:15

Growing Protein Crystals with Distinct Dimensions Using Automated Crystallization Coupled with In Situ Dynamic Light Scattering

Published on: August 14, 2018

11.1K
Protein Crystallization for X-ray Crystallography
09:27

Protein Crystallization for X-ray Crystallography

Published on: January 16, 2011

65.9K
Microcrystallography of Protein Crystals and In Cellulo Diffraction
09:35

Microcrystallography of Protein Crystals and In Cellulo Diffraction

Published on: July 21, 2017

9.6K

Area of Science:

  • Biophysics
  • Materials Science
  • Protein Crystallography

Background:

  • Proteins form various dense phases like gels and precipitates.
  • Noncrystalline protein phases are poorly understood and often assumed amorphous.
  • Crystalline protein structures are well-characterized, unlike other dense phases.

Purpose of the Study:

  • To investigate the nanostructure of ovalbumin precipitate particles.
  • To determine if noncrystalline protein dense phases possess ordered structures.
  • To challenge the assumption of amorphous protein gels.

Main Methods:

  • Small-angle neutron scattering (SANS)
  • Electron microscopy (EM)
  • Electron tomography

Main Results:

  • Ovalbumin phase-separates into core-shell particles (core radius ~2 μm, shell thickness ~0.5 μm).
  • The shell region exhibits nanostructures of ovalbumin crystallites.
  • These crystallites self-assemble into a bicontinuous network with ~12 nm thick branches.

Conclusions:

  • Ovalbumin precipitate particles are not fully amorphous.
  • Protein gels can contain nanocrystalline protein components.
  • The study reveals a self-assembled nanocrystalline network within protein precipitates.