Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Intrinsically Disordered Proteins

Intrinsically Disordered Proteins

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...

Intrinsically Disordered Proteins

Intrinsically Disordered Proteins

Dynamic Equilibrium

Dynamic Equilibrium

A reversible chemical reaction represents a chemical process that proceeds in both forward (left to right) and reverse (right to left) directions. When the rates of the forward and reverse reactions are equal, the concentrations of the reactant and product species remain constant over time and the system is at equilibrium. A special double arrow is used to emphasize the reversible nature of the reaction. The relative concentrations of reactants and products in equilibrium systems vary greatly;...

Protein Diffusion in the Membrane

Protein Diffusion in the Membrane

Proteins show rotational as well as lateral diffusion across the membrane. The lateral diffusion of proteins was confirmed through the cell fusion experiment where mouse and human cells were fused, resulting in hybrid cells. When the human and mouse cells fused, the specific membrane proteins on human and mouse cells were marked with the red and green-fluorescent markers, respectively. Initially, the red and green fluorescence was located on the respective hemisphere of the cell. As time...

Protein Dynamics in Living Cells

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 Transitions

Cooperative Allosteric Transitions

You might also read

Related Articles

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

Sort by

Same author

Exploring the structure and dynamics of peptide nanodiscs through a synergistic approach with NMR spectroscopy, SAS and MD simulations.

Communications chemistry·2026

Same author

Structure-Based Experimental Datasets for Benchmarking Protein Simulation Force Fields [Article v1.0].

Living journal of computational molecular science·2026

Same author

Molecular Dynamics of the Intrinsically Disordered Protein COR15A─A Force Field Validation on Structure and Dynamics.

Journal of chemical theory and computation·2025

Same author

Quality Evaluation Based Simulation Selection (QEBSS) for analysis of conformational ensembles and dynamics of multidomain proteins.

Communications chemistry·2025

Same author

Structure-Based Experimental Datasets for Benchmarking Protein Simulation Force Fields [Article v0.1].

ArXiv·2025

Same author

Rapid Interpretation of Protein Backbone Rotation Dynamics Directly from Spin Relaxation Data.

The journal of physical chemistry letters·2024

Search research articles

Related Experiment Video

Updated: Dec 9, 2025

Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments

Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments

Published on: November 1, 2024

Heterogeneous dynamics in partially disordered proteins.

Salla I Virtanen¹, Anne M Kiirikki¹, Kornelia M Mikula¹

¹Institute of Biotechnology, University of Helsinki, Helsinki, Finland. samuli.ollila@helsinki.fi.

Physical Chemistry Chemical Physics : PCCP

|September 15, 2020

Summary

Characterizing disordered protein regions is challenging. This study combines NMR spin relaxation and molecular dynamics simulations to reveal complex dynamics and conformational ensembles in partially disordered proteins like TonB.

More Related Videos

Study of Protein Dynamics via Neutron Spin Echo Spectroscopy

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

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

Published on: April 28, 2022

Related Experiment Videos

Last Updated: Dec 9, 2025

Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments

Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments

Published on: November 1, 2024

Study of Protein Dynamics via Neutron Spin Echo Spectroscopy

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

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

Published on: April 28, 2022

Area of Science:

Biophysics
Structural Biology
Protein Dynamics

Background:

Disordered protein regions are crucial in biology but difficult to study.
Existing experimental and theoretical methods have limitations in characterizing these regions.

Purpose of the Study:

To develop and demonstrate a combined approach using NMR spin relaxation and molecular dynamics (MD) simulations.
To characterize the heterogeneous dynamics and conformational ensembles of partially disordered proteins.

Main Methods:

Utilized protein backbone 15N spin relaxation data.
Integrated data with molecular dynamics (MD) simulations.
Applied segmental isotopic labeling with salt-inducible split intein.

Main Results:

Observed that folded regions exhibit rigid body rotation, independent of disordered linkers.
Disordered regions show complex, multi-timescale rotational motions (below ~30 ns).
Resolved the conformational ensemble and dynamics of the TonB protein's disordered periplasmic domain and chicken Engrailed 2.

Conclusions:

The combined MD simulations and NMR approach effectively captures complex dynamics of disordered regions.
This methodology provides insights into energy transfer mechanisms (e.g., TonB) and protein functions involving disordered domains.