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

Protein Dynamics in Living Cells01:19

Protein Dynamics in Living Cells

Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

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...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

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...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

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...
Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
Protein Folding01:25

Protein Folding

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...

You might also read

Related Articles

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

Sort by
Same author

Viral co-infection, autoimmunity, and CSF HIV antibody profiles in HIV central nervous system escape.

Journal of neuroimmunology·2023
Same author

Task-evoked pupillary responses track precision-weighted prediction errors and learning rate during interceptive visuomotor actions.

Scientific reports·2022
Same author

Integrating central nervous system metagenomics and host response for diagnosis of tuberculosis meningitis and its mimics.

Nature communications·2022
Same author

A Rare Bird: Diagnosis of Psittacosis Meningitis by Clinical Metagenomic Next-Generation Sequencing.

Open forum infectious diseases·2021
Same author

Neurite Orientation Dispersion and Density Imaging for Assessing Acute Inflammation and Lesion Evolution in MS.

AJNR. American journal of neuroradiology·2020
Same author

A theory for heterogeneous states of polymer melts produced by single chain crystal melting.

Soft matter·2020

Related Experiment Video

Updated: May 8, 2026

Study of Protein Dynamics via Neutron Spin Echo Spectroscopy
08:03

Study of Protein Dynamics via Neutron Spin Echo Spectroscopy

Published on: April 13, 2022

Allostery without conformation change: modelling protein dynamics at multiple scales.

T C B McLeish1, T L Rodgers, M R Wilson

  • 1Biophysical Sciences Institute, Durham University, South Road, Durham DH1 3LE, UK.

Physical Biology
|September 12, 2013
PubMed
Summary

Protein dynamics can enable allosteric signaling through fluctuations, not just structural changes. A key requirement for this fluctuation-induced allostery is an inhomogeneous elastic modulus in proteins.

More Related Videos

High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water
08:48

High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water

Published on: April 28, 2022

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

Related Experiment Videos

Last Updated: May 8, 2026

Study of Protein Dynamics via Neutron Spin Echo Spectroscopy
08:03

Study of Protein Dynamics via Neutron Spin Echo Spectroscopy

Published on: April 13, 2022

High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water
08:48

High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water

Published on: April 28, 2022

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

Area of Science:

  • Biophysics
  • Structural Biology
  • Protein Dynamics

Background:

  • Allosteric signaling in proteins is crucial for biological regulation.
  • The Monod-Wyman-Changeux (MWC) model explains allostery via conformational shifts.
  • Cooper and Dryden proposed an alternative: allostery via modulation of thermal fluctuations.

Purpose of the Study:

  • To theoretically identify structural requirements for fluctuation-induced allostery.
  • To extend coarse-grained models to more detailed protein dynamics.
  • To understand the physical basis of allosteric signaling beyond conformational changes.

Main Methods:

  • Theoretical modeling approach, progressing from coarse-grained to detailed representations.
  • Analysis of protein elastic properties and their relationship to dynamics.
  • Review and extension of existing theoretical frameworks for allostery.

Main Results:

  • A strongly inhomogeneous elastic modulus is a fundamental requirement for fluctuation-induced allostery.
  • Real proteins often exhibit this property, with rigid domains connected by flexible interfaces.
  • This inhomogeneous elasticity supports allosteric signaling through amplitude modulation of thermal fluctuations.

Conclusions:

  • Protein dynamics, specifically thermal fluctuations, can mediate allosteric signaling.
  • Inhomogeneous elastic modulus is a critical structural determinant for this mechanism.
  • This provides a complementary perspective to traditional allostery models like MWC.