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

Globular and Fibrous Proteins02:21

Globular and Fibrous Proteins

4.0K
4.0K
Globular Proteins01:27

Globular Proteins

7.1K
In organisms, proteins are the most abundant macromolecules. They act as the building blocks of life and play various crucial roles in the body. Proteins can be broadly classified into two distinct subtypes based on their shape and solubilities: globular proteins and fibrous proteins.
Globular proteins serve many important physiological functions, such as acting as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be soluble in the aqueous...
7.1K
Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

17.7K
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...
17.7K
Protein Dynamics in Living Cells01:19

Protein Dynamics in Living Cells

2.1K
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...
2.1K
Protein Diffusion in the Membrane01:24

Protein Diffusion in the Membrane

4.3K
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...
4.3K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

17.7K
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...
17.7K

You might also read

Related Articles

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

Sort by
Same author

Shadow Hamiltonian in molecular dynamics simulations: Against a possible suggested misuse of its physical meaning.

The Journal of chemical physics·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

Destabilizing Interactions in Human Telomeric G-Quadruplex Multimers.

The journal of physical chemistry letters·2025
Same author

Polymeric Properties of Telomeric G-Quadruplex Multimers: Effects of Chemically Inert Crowders.

Biomacromolecules·2025
Same author

In silico study of DNA mononucleotide self-assembly.

The Journal of chemical physics·2024
Same author

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

APL bioengineering·2024
Same journal

Nanopore sequencing with proteins: synchronization and dischronization of molecular dynamics simulations with laboratory and industrial developments.

Soft matter·2026
Same journal

Catanionics from biosurfactants and regular surfactants: miscibility and structure.

Soft matter·2026
Same journal

Adhesives with a thickness smaller than the fractocohesive length enhance adhesion.

Soft matter·2026
Same journal

Non-equilibrium phase transitions in hybrid Voronoi models of cell colonies.

Soft matter·2026
Same journal

Effects of methoxy substituents on self-assembly and gelation performance of benzamide-based organogelators.

Soft matter·2026
Same journal

Rheology of <i>Escherichia coli</i> suspensions with various bacterial morphologies and motion characteristics.

Soft matter·2026
See all related articles

Related Experiment Video

Updated: Jun 2, 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

2.0K

Dynamical arrest for globular proteins with patchy attractions.

Maxime J Bergman1, Tommy Garting1, Cristiano De Michele2

  • 1Division of Physical Chemistry, Department of Chemistry, Lund University, PO Box 124, SE-221 00 Lund, Sweden. peter.schurtenberger@fkem1.lu.se.

Soft Matter
|January 17, 2025
PubMed
Summary
This summary is machine-generated.

Researchers studied concentrated eye lens protein solutions, finding that simple colloid models fail to fully explain their complex dynamics. Novel findings highlight the limitations of current models in predicting protein solution behavior, especially concerning viscosity and gel formation.

More Related Videos

Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments
09:25

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

Published on: November 1, 2024

1.7K
Using SecM Arrest Sequence as a Tool to Isolate Ribosome Bound Polypeptides
09:42

Using SecM Arrest Sequence as a Tool to Isolate Ribosome Bound Polypeptides

Published on: June 19, 2012

12.3K

Related Experiment Videos

Last Updated: Jun 2, 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

2.0K
Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments
09:25

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

Published on: November 1, 2024

1.7K
Using SecM Arrest Sequence as a Tool to Isolate Ribosome Bound Polypeptides
09:42

Using SecM Arrest Sequence as a Tool to Isolate Ribosome Bound Polypeptides

Published on: June 19, 2012

12.3K

Area of Science:

  • Colloid and Surface Science
  • Biophysics
  • Soft Matter Physics

Background:

  • Concentrated protein solutions exhibit complex dynamics challenging colloid science models.
  • Globular proteins have heterogeneous surfaces, leading to anisotropic interactions.
  • Understanding non-equilibrium transitions like glass and gel formation is crucial.

Purpose of the Study:

  • To systematically study the reduced zero shear viscosity (ηr) of gamma B-crystallin, an eye lens protein.
  • To compare experimental results with existing structural and dynamic data.
  • To investigate the concentration and temperature dependence of viscosity and locate the kinetic arrest line.

Main Methods:

  • Utilized two distinct tracer particle-based microrheology techniques.
  • Precisely mapped the kinetic arrest line within the phase diagram.
  • Characterized the functional form of viscosity dependence on concentration and temperature.

Main Results:

  • Results qualitatively align with patchy colloid models for gamma B-crystallin.
  • Identified novel findings not explained by simple colloid models.
  • Demonstrated the failure of the extended law of corresponding states for the arrest line's temperature dependence.

Conclusions:

  • Gamma B-crystallin behavior is complex and not fully captured by current simple colloid models.
  • Transient clusters likely play a significant role in the observed dynamics.
  • Further refinement of colloid models is needed for crowded protein solutions.