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

Structural Protein Function01:56

Structural Protein Function

27.5K
Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity.  In bones and teeth, it mineralizes to...
27.5K
Protein Folding01:22

Protein Folding

117.6K
Overview
117.6K
Assembly of Cytoskeletal Filaments01:18

Assembly of Cytoskeletal Filaments

18.5K
Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...
18.5K
Amyloid Fibrils03:03

Amyloid Fibrils

9.3K
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,...
9.3K
Protein Complex Assembly02:41

Protein Complex Assembly

10.6K
Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
10.6K
Assembly of Complex Microtubule Structures01:32

Assembly of Complex Microtubule Structures

1.8K
Complex microtubule structures are present in resting cells and in dividing cells. In resting cells, they are responsible for maintaining the cellular architecture, tracks for intracellular transport, positioning of organelles, assembly of cilia and flagella. They mediate the bipolar spindle assembly for chromosomal segregation and positioning of the cell division plate in dividing cells. The formation of microtubule complex structures depends on the cell type, cell stage, and cell function.
1.8K

You might also read

Related Articles

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

Sort by
Same author

S-layers as natural building blocks for nanobiotechnology and synthetic biology.

Current opinion in microbiology·2026
Same author

Crucial Gram-positive type IV secretion system protein TraF is a structural homolog of type VII secretion system protein EssB/YukC.

microLife·2026
Same author

Guiding AlphaFold predictions with experimental knowledge to inform dynamics and interactions with VAIRO.

Protein science : a publication of the Protein Society·2026
Same author

Major Cat Allergen Fel d 4: Structure and Identification of a Cross-Reactive IgE-Epitope-Containing Area.

Allergy·2025
Same author

A Single-Domain VNAR Nanobody Binds with High-Affinity and Selectivity to the Heparin Pentasaccharide Fondaparinux.

International journal of molecular sciences·2025
Same author

Structural basis of phosphorylation-independent nuclear import of CIRBP by TNPO3.

Nature communications·2025

Related Experiment Video

Updated: Jun 12, 2025

A Protocol for Computer-Based Protein Structure and Function Prediction
16:41

A Protocol for Computer-Based Protein Structure and Function Prediction

Published on: November 3, 2011

68.6K

SymProFold: Structural prediction of symmetrical biological assemblies.

Christoph Buhlheller1,2, Theo Sagmeister1, Christoph Grininger1

  • 1Institute of Molecular Biosciences, University of Graz, Graz, Austria.

Nature Communications
|September 18, 2024
PubMed
Summary

SymProFold predicts symmetrical protein assemblies like bacterial S-layers and viral capsids using AlphaFold-Multimer. This computational tool aids in understanding protein functions and designing new applications.

More Related Videos

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
07:08

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Published on: July 14, 2015

7.3K
Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry
05:58

Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry

Published on: July 17, 2019

11.0K

Related Experiment Videos

Last Updated: Jun 12, 2025

A Protocol for Computer-Based Protein Structure and Function Prediction
16:41

A Protocol for Computer-Based Protein Structure and Function Prediction

Published on: November 3, 2011

68.6K
Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
07:08

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Published on: July 14, 2015

7.3K
Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry
05:58

Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry

Published on: July 17, 2019

11.0K

Area of Science:

  • Structural biology
  • Computational biology
  • Biophysics

Background:

  • Symmetrical protein assemblies, such as bacterial cell surface layers (S-layers), are crucial for cellular functions including adhesion and immune evasion.
  • Experimental characterization of these self-assembling structures is difficult due to inherent properties and sequence diversity.
  • Understanding the symmetry of these protein arrays is key to deciphering their biological roles.

Purpose of the Study:

  • To introduce the SymProFold pipeline for predicting symmetrical protein assemblies.
  • To leverage AlphaFold-Multimer predictions for deriving 2D S-layer arrays and spherical viral capsids.
  • To validate predicted symmetries against experimental data and crystal structures.

Main Methods:

  • Utilized AlphaFold-Multimer for high-accuracy protein structure prediction.
  • Developed the SymProFold pipeline to test and identify known symmetry operations (p1, p2, p3, p4, p6).
  • Validated computational models with existing cellular data and confirmed interfaces via crystal structures.

Main Results:

  • SymProFold successfully predicts symmetrical protein assemblies, including S-layer arrays and viral capsids.
  • The pipeline accurately identifies the most probable symmetry for a given protein sequence.
  • Experimental validation confirmed the predicted symmetries and interfaces of multiple assemblies.

Conclusions:

  • The SymProFold pipeline provides a robust method for determining the structure of symmetric protein assemblies.
  • This tool facilitates the exploration of protein functionalities and enables the design of targeted applications.
  • Opens new avenues in nanotechnology, biotechnology, medicine, and materials science through the study of symmetric protein structures.