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

Dynamic Equilibrium02:20

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;...
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...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

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 to...
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...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

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 to...

You might also read

Related Articles

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

Sort by
Same author

Non-Fickian diffusion within assemblies of the intrinsically disordered protein β-casein.

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

Structure and Chain Dynamics of Self-Healing Telechelic Polymer Networks.

Macromolecules·2026
Same author

Electrostatics and viscosity are strongly linked in concentrated antibody solutions.

Proceedings of the National Academy of Sciences of the United States of America·2025
Same author

Dynamical arrest for globular proteins with patchy attractions.

Soft matter·2025
Same author

Continuity of Short-Time Dynamics Crossing the Liquid-Liquid Phase Separation in Charge-Tuned Protein Solutions.

The journal of physical chemistry letters·2024
Same author

Confined bicontinuous microemulsions: nanoscale dynamics of the surfactant film.

Soft matter·2024
Same journal

Shape factor analysis as a quantitative framework for assessing spheroid and organoid morphology and invasiveness.

APL bioengineering·2026
Same journal

HB-EGF enhances collective cell migration via spatial coordination of traction.

APL bioengineering·2026
Same journal

A pump-free microfluidic device for integrated multi-functional testing of tumor spheroids.

APL bioengineering·2026
Same journal

Photobiomodulation outperforms ultrasound in reducing IL-1 <b><i>β</i></b> -driven chondrocyte inflammation.

APL bioengineering·2026
Same journal

Research progress of 3D-printed anti-infective bone tissue engineering scaffolds based on triply periodic minimal surface structures.

APL bioengineering·2026
Same journal

Biomolecular and cellular chirality: Novel diagnostic perspectives for diseases.

APL bioengineering·2026
See all related articles

Related Experiment Video

Updated: Jun 14, 2026

T-wave Ion Mobility-mass Spectrometry: Basic Experimental Procedures for Protein Complex Analysis
16:40

T-wave Ion Mobility-mass Spectrometry: Basic Experimental Procedures for Protein Complex Analysis

Published on: July 31, 2010

24.6K

Testing mixing rules for structural and dynamical quantities in multi-component crowded protein solutions.

Alessandro Gulotta1, Saskia Bucciarelli1, Felix Roosen-Runge

  • 1Division for Physical Chemistry, Lund University, Naturvetarvägen 14, 22100 Lund, Sweden.

APL Bioengineering
|June 3, 2024
PubMed
Summary
This summary is machine-generated.

Predicting protein mixture behavior is challenging. Simple mixing rules can describe macroscopic properties of protein solutions, but individual protein size requires more interaction data.

More Related Videos

Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies
10:01

Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies

Published on: November 28, 2017

19.7K
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

2.1K

Related Experiment Videos

Last Updated: Jun 14, 2026

T-wave Ion Mobility-mass Spectrometry: Basic Experimental Procedures for Protein Complex Analysis
16:40

T-wave Ion Mobility-mass Spectrometry: Basic Experimental Procedures for Protein Complex Analysis

Published on: July 31, 2010

24.6K
Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies
10:01

Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies

Published on: November 28, 2017

19.7K
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

2.1K

Area of Science:

  • Biophysics
  • Soft Matter Physics
  • Biochemistry

Background:

  • Concentrated protein mixtures in cytoplasm and serum exhibit complex phase behavior and properties.
  • Theoretical prediction of these systems is difficult due to crowding effects.
  • Existing models effectively describe monodisperse protein solutions but not polydisperse mixtures.

Purpose of the Study:

  • To evaluate the efficacy of simple mixing rules for predicting the solution properties of protein mixtures.
  • To investigate the behavior of binary mixtures of alpha-crystallin and gamma-crystallin.

Main Methods:

  • Microrheology
  • Static and dynamic scattering techniques
  • Liquid-liquid phase separation analysis

Main Results:

  • Simple mixing rules provide reasonably accurate predictions for macroscopic and mesoscopic properties of protein mixtures.
  • Accurate description of individual protein size requires detailed information on cross-component interactions.
  • The study successfully characterized the phase diagram and solution properties of the model protein system.

Conclusions:

  • Simple mixing rules offer a viable approach for predicting bulk properties of protein mixtures.
  • Understanding molecular-level interactions is crucial for predicting finer details like individual protein size.
  • This research advances theoretical models for complex biological fluid behavior.