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

18.2K
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...
18.2K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

18.5K
The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
18.5K
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

2.6K
Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...
2.6K
Protein Organization01:24

Protein Organization

7.2K
Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence....
7.2K
Protein Folding01:22

Protein Folding

121.5K
Overview
121.5K
Protein Dynamics in Living Cells01:19

Protein Dynamics in Living Cells

2.3K
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...
2.3K

You might also read

Related Articles

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

Sort by
Same author

Proteome-scale quantification of the interactions driving condensate formation of intrinsically disordered proteins.

Nature communications·2026
Same author

Integrated NMR/MD investigation reveals differences after reweighting in conformational ensembles of GAAG and GCAA tetraloops.

RNA (New York, N.Y.)·2026
Same author

Effects of residue substitutions on the cellular abundance of proteins.

eLife·2026
Same author

StruCloze: A Unified Framework for Backmapping and Inpainting Biomolecule Structures.

Journal of chemical theory and computation·2026
Same author

A Stickiness Scale for Disordered Proteins.

The journal of physical chemistry. B·2026
Same author

Transient tertiary structure in intrinsically disordered proteins revealed by multithermal enhanced sampling.

Nature communications·2026

Related Experiment Video

Updated: Sep 15, 2025

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

2.2K

A coarse-grained model for disordered proteins under crowded conditions.

Arriën Symon Rauh1, Giulio Tesei1, Kresten Lindorff-Larsen1

  • 1Structural Biology and NMR Laboratory, Linderstrøm-Lang Centre for Protein Science, Department of Biology, University of Copenhagen, Copenhagen, Denmark.

Protein Science : a Publication of the Protein Society
|July 17, 2025
PubMed
Summary

Macromolecular crowding significantly impacts protein dynamics and function. This study introduces a new coarse-grained model for polyethylene glycol (PEG) to quantify protein phase separation propensities in crowded environments.

Keywords:
PEGcondensatescrowdingintrinsically disordered proteins

More Related Videos

Author Spotlight: Evaluation of Protein-Condensate Dynamics in Live Human Cells
06:48

Author Spotlight: Evaluation of Protein-Condensate Dynamics in Live Human Cells

Published on: January 5, 2024

4.1K
Structure-Based Simulation and Sampling of Transcription Factor Protein Movements along DNA from Atomic-Scale Stepping to Coarse-Grained Diffusion
09:17

Structure-Based Simulation and Sampling of Transcription Factor Protein Movements along DNA from Atomic-Scale Stepping to Coarse-Grained Diffusion

Published on: March 1, 2022

3.3K

Related Experiment Videos

Last Updated: Sep 15, 2025

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

2.2K
Author Spotlight: Evaluation of Protein-Condensate Dynamics in Live Human Cells
06:48

Author Spotlight: Evaluation of Protein-Condensate Dynamics in Live Human Cells

Published on: January 5, 2024

4.1K
Structure-Based Simulation and Sampling of Transcription Factor Protein Movements along DNA from Atomic-Scale Stepping to Coarse-Grained Diffusion
09:17

Structure-Based Simulation and Sampling of Transcription Factor Protein Movements along DNA from Atomic-Scale Stepping to Coarse-Grained Diffusion

Published on: March 1, 2022

3.3K

Area of Science:

  • Biophysics
  • Computational Biology
  • Protein Dynamics

Background:

  • Macromolecular crowding profoundly influences protein dynamics and function, especially for intrinsically disordered proteins.
  • Understanding crowding effects on protein chain compaction and phase separation (PS) is crucial for biological function.
  • Previous studies utilized synthetic crowders like polyethylene glycol (PEG) and ficoll, alongside theoretical models and simulations.

Purpose of the Study:

  • To develop a residue-based coarse-grained model for PEG compatible with the CALVADOS protein model.
  • To optimize PEG model parameters using experimental data on PEG's single-chain behavior and its effect on protein compaction.
  • To quantify phase separation propensities of proteins with weak PS tendencies using the developed PEG model.

Main Methods:

  • Developed a residue-based coarse-grained model for polyethylene glycol (PEG).
  • Optimized PEG model parameters by comparing simulation data with experimental results.
  • Applied the model to study PEG-induced compaction and phase separation of disordered proteins.

Main Results:

  • The developed PEG model accurately reproduces experimental data on PEG compaction of disordered proteins.
  • PEG titrations effectively quantify phase separation propensities, even for proteins with weak tendencies.
  • Crowding response to PEG varied between charge patterning variants of α-synuclein, but not for aromatic residue variants in A1-LCD.

Conclusions:

  • The new PEG model aids in interpreting crowding experiments with disordered proteins.
  • This model serves as a foundation for studying proteins with weak phase separation propensities.
  • The findings highlight the differential impact of crowding on protein variants based on their sequence features.