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

Mechanisms of Membrane-bending01:15

Mechanisms of Membrane-bending

The living membranes are flexible due to their fluid mosaic nature; however, their bending into different shapes is an active process regulated by specific lipids and proteins. The membrane bending can be transient as seen in vesicles or stable for a long time as in microvilli. Cells regulate the size, location, and duration of the membrane curvature.
Membrane bending can happen due to intrinsic changes in lipid composition or extrinsic association with different proteins. The proteins involved...
Protein-protein Interfaces02:04

Protein-protein Interfaces

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 polypeptide...
Protein-Protein Interfaces02:04

Protein-Protein Interfaces

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 polypeptide...
Multi-pass Transmembrane Proteins and β-barrels01:09

Multi-pass Transmembrane Proteins and β-barrels

In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as G-protein-linked receptors (GPCRs) and...
Ligand Binding and Linkage00:49

Ligand Binding and Linkage

Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence the...
Structural Protein Function01:56

Structural Protein Function

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 form...

You might also read

Related Articles

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

Sort by
Same author

MD2NMR: Linking molecular dynamics with NMR relaxation.

Biophysical journal·2026
Same author

Case Report: Rare pheochromocytoma in a patient with Li-Fraumeni syndrome: a 3-event, 4-hit model of pathogenesis.

Frontiers in oncology·2026
Same author

Intracranial mesenchymal tumor, FET::CREB fusion-positive: An integrative analysis of 81 cases.

Neuro-oncology·2026
Same author

Integrating evidence from protein domains to identify cancer driver mutations.

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

G34R cancer mutation alters the conformational ensemble and dynamics of the histone H3.3 tails.

Nucleic acids research·2026
Same author

Pediatric-Type Follicular Lymphoma of the Conjunctiva: Shared Histologic and Molecular Features With the Nodal Counterpart.

The American journal of surgical pathology·2025

Related Experiment Video

Updated: Jun 21, 2026

Pulling Membrane Nanotubes from Giant Unilamellar Vesicles
06:26

Pulling Membrane Nanotubes from Giant Unilamellar Vesicles

Published on: December 7, 2017

Exploring functional roles of multibinding protein interfaces.

Manoj Tyagi1, Benjamin A Shoemaker, Stephen H Bryant

  • 1Computational Biology Branch, National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, Maryland 20894, USA.

Protein Science : a Publication of the Protein Society
|July 11, 2009
PubMed
Summary

Multibinding proteins, which interact with diverse partners using shared interfaces, are rare (5% of families). Their interfaces lack high sequence conservation but employ specific mechanisms for functional switching and partner recognition.

More Related Videos

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
09:51

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

Published on: July 16, 2017

Pulldown Assay Coupled with Co-Expression in Bacteria Cells as a Time-Efficient Tool for Testing Challenging Protein-Protein Interactions
07:03

Pulldown Assay Coupled with Co-Expression in Bacteria Cells as a Time-Efficient Tool for Testing Challenging Protein-Protein Interactions

Published on: December 23, 2022

Related Experiment Videos

Last Updated: Jun 21, 2026

Pulling Membrane Nanotubes from Giant Unilamellar Vesicles
06:26

Pulling Membrane Nanotubes from Giant Unilamellar Vesicles

Published on: December 7, 2017

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
09:51

Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web

Published on: July 16, 2017

Pulldown Assay Coupled with Co-Expression in Bacteria Cells as a Time-Efficient Tool for Testing Challenging Protein-Protein Interactions
07:03

Pulldown Assay Coupled with Co-Expression in Bacteria Cells as a Time-Efficient Tool for Testing Challenging Protein-Protein Interactions

Published on: December 23, 2022

Area of Science:

  • Molecular biology
  • Structural biology
  • Biochemistry

Background:

  • Cellular processes involve interconnected pathways with shared proteins.
  • Multibinding proteins utilize the same interface regions to interact with diverse partners.

Purpose of the Study:

  • Decipher mechanisms of molecular recognition by promiscuous protein regions.
  • Analyze physicochemical properties of multibinding interfaces.
  • Highlight functional switches mediated by multibinding.

Main Methods:

  • Analysis of protein structure database.
  • Characterization of physicochemical properties of protein interfaces.
  • Identification of sequence conservation patterns.

Main Results:

  • Only 5% of protein families possess multibinding interfaces.
  • Multibinding interfaces show no higher sequence conservation than background sites.
  • Identified functional mechanisms including pathway overlap prevention, sequential substrate transfer, specificity modulation, and inhibitor binding via mimicry.

Conclusions:

  • Multibinding proteins employ specific strategies to manage interactions with diverse partners.
  • Functional switches and specificity regulation are key roles of these interfaces.
  • Understanding these mechanisms is crucial for comprehending complex cellular networks.