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

Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

17.8K
Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
17.8K
Cytoskeletal Accessory Proteins01:13

Cytoskeletal Accessory Proteins

3.1K
The cytoskeleton is an essential cell component that plays several structural and functional roles. However, the filaments that make up the cytoskeleton cannot function independently and depend on the accessory or ancillary proteins to effectively carry out their function. Accessory proteins associate with cytoskeletal filaments and their monomers, aiding filament formation and function. They also help in the cross-communication among cytoskeletal filaments. Cytoskeletal accessory proteins are...
3.1K
Protein-protein Interfaces02:04

Protein-protein Interfaces

12.5K
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...
12.5K
Mechanisms of Membrane-bending01:15

Mechanisms of Membrane-bending

2.7K
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...
2.7K
Protein Folding01:22

Protein Folding

118.1K
Overview
118.1K
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

5.8K
Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
5.8K

You might also read

Related Articles

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

Sort by
Same author

Probing Charge-Controlled Inter-Domain Flexibility: Integrating Experimental and Coarse-Grained Approaches.

Journal of chemical information and modeling·2026
Same author

Cancer-linked aggregation of p53 is driven by sequence-encoded frustration, solvation, and hydrophobic gating absent in its paralogs.

Communications chemistry·2026
Same author

Small Molecule Regulation of CLOCK:BMAL1 DNA Binding Activity.

bioRxiv : the preprint server for biology·2026
Same author

Structural Basis of a Novel Heme Binding Bacterial One-Component Switch.

bioRxiv : the preprint server for biology·2026
Same author

NMR Based Real-Time Analysis of Exometabolites Decodes the Mechanism of Action of Antibacterial Molecules, Nanoparticles, and Materials.

Analytical chemistry·2026
Same author

A data-driven chromatin model reveals spatial and dynamic features of genome organization.

Proceedings of the National Academy of Sciences of the United States of America·2026

Related Experiment Video

Updated: Jun 30, 2025

Time-Resolved Fluorescence Anisotropy from Single Molecules for Characterizing Local Flexibility in Biomolecules
10:23

Time-Resolved Fluorescence Anisotropy from Single Molecules for Characterizing Local Flexibility in Biomolecules

Published on: April 25, 2025

240

Uncovering the Association Mechanism between Two Intrinsically Flexible Proteins.

Angy Liseth Dávalos1, José David Rivera Echeverri1, Denize C Favaro2,3

  • 1Department of Biochemistry, Institute of Chemistry, University of São Paulo, São Paulo, 05508-000, Brazil.

ACS Chemical Biology
|March 15, 2024
PubMed
Summary

The VirB9 C-terminal domain (VirB9Ct) and VirB7 N-terminal motif (VirB7Nt) interaction involves coupled folding and binding. Temperature influences this mechanism, affecting pathways to the final complex.

More Related Videos

OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy
08:34

OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy

Published on: February 5, 2020

6.7K
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

Related Experiment Videos

Last Updated: Jun 30, 2025

Time-Resolved Fluorescence Anisotropy from Single Molecules for Characterizing Local Flexibility in Biomolecules
10:23

Time-Resolved Fluorescence Anisotropy from Single Molecules for Characterizing Local Flexibility in Biomolecules

Published on: April 25, 2025

240
OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy
08:34

OaAEP1-Mediated Enzymatic Synthesis and Immobilization of Polymerized Protein for Single-Molecule Force Spectroscopy

Published on: February 5, 2020

6.7K
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

Area of Science:

  • Structural Biology
  • Biochemistry
  • Molecular Biology

Background:

  • Protein-protein interactions are crucial for cell signaling and drug development.
  • Intrinsically disordered proteins (IDPs) folding upon binding is a key research area.
  • The VirB9 C-terminal domain (VirB9Ct) and VirB7 N-terminal motif (VirB7Nt) form part of the Type IV Secretion System injectisome.

Purpose of the Study:

  • To characterize the coupled folding and binding mechanism between VirB9Ct and VirB7Nt.
  • To investigate the influence of temperature on this interaction.
  • To elucidate the role of conformational dynamics in the binding process.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) spectroscopy
  • Stopped-flow fluorescence
  • Computer simulations using structure-based models

Main Results:

  • VirB9Ct is intrinsically dynamic in its free state, while VirB7Nt is a random coil.
  • Conformational selection is favored at lower temperatures for VirB9Ct-VirB7Nt binding.
  • Higher temperatures allow for alternative pathways involving non-native complexes due to easier surmounting of energy barriers.

Conclusions:

  • The folding and binding of VirB9Ct and VirB7Nt are intimately linked.
  • The interaction occurs on a complex energy landscape with multiple potential intermediates.
  • Temperature-dependent mechanisms dictate the search for favored intramolecular and intermolecular interactions.