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

Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

9.3K
Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
9.3K
Induced-fit Model01:13

Induced-fit Model

91.1K
Most chemical reactions in cells require enzymes—biological catalysts that speed up the reaction without being consumed or permanently changed. They reduce the activation energy needed to convert the reactants into products. Enzymes are proteins, that usually work by binding to a substrate—a reactant molecule that they act upon.
Enzymes exhibit substrate specificity, meaning that they can only bind to certain substrates. This is mainly determined by the shape and chemical...
91.1K
Protein Complex Assembly02:41

Protein Complex Assembly

17.0K
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...
17.0K
Protein-protein Interfaces02:04

Protein-protein Interfaces

14.9K
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...
14.9K
Protein Folding01:25

Protein Folding

12.0K
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...
12.0K
Protein Folding01:22

Protein Folding

129.7K
Overview
129.7K

You might also read

Related Articles

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

Sort by
Same author

Harnessing artificial intelligence for the assessment of liver fibrosis and steatosis <i>via</i> multiparametric ultrasound.

World journal of gastroenterology·2026
Same author

Advances in endoscopic ultrasound-guided shear wave elastography: A comprehensive review of its clinical applications.

World journal of gastroenterology·2026
Same author

Shear wave elastography in healthy patients: Pancreatic stiffness is less reliable than liver and spleen measurements.

World journal of radiology·2025
Same author

Multiparametric ultrasound for the prediction of the short-term outcome after esophageal varices band ligation.

World journal of gastroenterology·2025
Same author

A Scoring Function for Monolayer-Protected Gold Nanoparticles Capable of Recognizing Small Organic Molecules in Solution.

Journal of chemical theory and computation·2025
Same author

Multiparametric ultrasound for non-invasive assessment of liver steatosis, fibrosis, and inflammation in metabolic dysfunction-associated steatotic liver disease.

World journal of gastroenterology·2025

Related Experiment Video

Updated: Mar 12, 2026

Calibration-free In Vitro Quantification of Protein Homo-oligomerization Using Commercial Instrumentation and Free, Open Source Brightness Analysis Software
08:22

Calibration-free In Vitro Quantification of Protein Homo-oligomerization Using Commercial Instrumentation and Free, Open Source Brightness Analysis Software

Published on: July 17, 2018

7.8K

Induced Fit in Protein Multimerization: The HFBI Case.

Laura Riccardi1, Paolo Mereghetti2

  • 1Laboratory of Molecular Modeling and Drug Discovery, Istituto Italiano di Tecnologia, Genoa, Italy.

Plos Computational Biology
|November 11, 2016
PubMed
Summary

Hydrophobins are fungal proteins with surface activity. This study reveals how a flexible hairpin in hydrophobin II (HFBI) controls its multimerization, impacting biological functions and applications.

More Related Videos

Multimer-PAGE: A Method for Capturing and Resolving Protein Complexes in Biological Samples
07:40

Multimer-PAGE: A Method for Capturing and Resolving Protein Complexes in Biological Samples

Published on: May 5, 2017

12.1K
Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library
10:17

Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library

Published on: January 14, 2020

8.3K

Related Experiment Videos

Last Updated: Mar 12, 2026

Calibration-free In Vitro Quantification of Protein Homo-oligomerization Using Commercial Instrumentation and Free, Open Source Brightness Analysis Software
08:22

Calibration-free In Vitro Quantification of Protein Homo-oligomerization Using Commercial Instrumentation and Free, Open Source Brightness Analysis Software

Published on: July 17, 2018

7.8K
Multimer-PAGE: A Method for Capturing and Resolving Protein Complexes in Biological Samples
07:40

Multimer-PAGE: A Method for Capturing and Resolving Protein Complexes in Biological Samples

Published on: May 5, 2017

12.1K
Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library
10:17

Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library

Published on: January 14, 2020

8.3K

Area of Science:

  • Biochemistry
  • Protein Science
  • Fungal Biology

Background:

  • Hydrophobins are small amphipathic proteins from filamentous fungi.
  • Their biological functions and technological applications depend on surface-activity properties.
  • Understanding hydrophobin multimerization is crucial for clarifying their interfacial activity.

Purpose of the Study:

  • To investigate the role of a flexible β-hairpin in the multimerization of hydrophobin II from Trichoderma reesei (HFBI).
  • To characterize how β-hairpin displacement influences the stability of HFBI monomers, dimers, and tetramers.
  • To propose mechanisms for HFBI multimerization in solution.

Main Methods:

  • Free energy calculations were employed to study the multimerization process.
  • The stability of different HFBI oligomeric states (monomers, dimers, tetramers) was analyzed.
  • The influence of a flexible β-hairpin on protein-protein interactions was characterized.

Main Results:

  • A flexible β-hairpin plays a key role in regulating HFBI multimerization.
  • The displacement of this β-hairpin controls the stability of HFBI oligomers in solution.
  • This study describes a novel mechanism involving a flexible loop and a hydrophobic patch in protein-protein binding.

Conclusions:

  • The regulation of HFBI oligomerization equilibrium directly affects its interfacial properties.
  • Understanding this mechanism is vital for both the biological function and technological applications of hydrophobins.
  • This work presents the first description of a flexible loop controlling protein-protein binding within a hydrophobic patch.