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

You might also read

Related Articles

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

Sort by

Same author

The importance of being heterogeneous: the complex phase behaviour of insect cuticular hydrocarbons.

Journal of the Royal Society, Interface·2025

Same author

Molecular rotors in haemoglobin and bovine serum albumin proteins.

Journal of the Royal Society, Interface·2022

Same author

Molecular rotors as intracellular probes of red blood cell stiffness.

Soft matter·2021

See all related articles

Search research articles

Related Experiment Video

Updated: May 16, 2025

Study of Protein Dynamics via Neutron Spin Echo Spectroscopy

Study of Protein Dynamics via Neutron Spin Echo Spectroscopy

Published on: April 13, 2022

Slow and fluctuating dynamics in high concentration BSA protein solutions.

A Briole¹, B Abou¹

¹Matière et Systèmes Complexes, UMR7057 CNRS - Université Paris Cité, 75205 Paris, France.

The Journal of Chemical Physics

|April 1, 2025

Summary

This study investigated bovine serum albumin (BSA) solutions, finding that viscosity and relaxation times increase with concentration. At very high concentrations, BSA solutions behave like soft colloids, showing mild increases in relaxation times.

More Related Videos

Characterization of Proteins by Size-Exclusion Chromatography Coupled to Multi-Angle Light Scattering SEC-MALS

Characterization of Proteins by Size-Exclusion Chromatography Coupled to Multi-Angle Light Scattering SEC-MALS

Published on: June 20, 2019

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: May 16, 2025

Study of Protein Dynamics via Neutron Spin Echo Spectroscopy

Study of Protein Dynamics via Neutron Spin Echo Spectroscopy

Published on: April 13, 2022

Characterization of Proteins by Size-Exclusion Chromatography Coupled to Multi-Angle Light Scattering SEC-MALS

Characterization of Proteins by Size-Exclusion Chromatography Coupled to Multi-Angle Light Scattering SEC-MALS

Published on: June 20, 2019

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
Soft Matter Physics
Materials Science

Background:

Bovine serum albumin (BSA) is a widely studied globular protein.
Understanding protein solution dynamics is crucial for various applications.
High protein concentrations present unique challenges in characterizing solution behavior.

Purpose of the Study:

To investigate the rheological properties and dynamics of BSA solutions across a broad concentration range.
To explore the phase behavior and molecular motions in concentrated BSA solutions.
To compare the behavior of BSA solutions to other soft matter systems.

Main Methods:

Particle tracking microrheology
Dynamic light scattering
Bradford assay for precise concentration control

Main Results:

Viscosity and relaxation times increase significantly with BSA concentration.
At very high concentrations, BSA solutions exhibit behavior similar to soft colloids.
Temperature-quenched dynamics reveal a mild aging regime with micro-rearrangements.

Conclusions:

BSA solutions display complex phase behavior and dynamics at high concentrations.
The findings offer insights into protein solution behavior relevant to biophysics and materials science.
This study provides a foundation for further research into concentrated protein systems.