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Related Concept Videos

Protein Diffusion in the Membrane01:24

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...
Intrinsically Disordered Proteins02:18

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 Proteins02:18

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...
Amyloid Fibrils03:03

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...
Protein Dynamics in Living Cells01:19

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...
Overview of Protein Sorting and Transport01:45

Overview of Protein Sorting and Transport

Eukaryotic cells have different membrane-bound organelles with distinct protein requirements. The process by which proteins are targeted to a specific organelle is called protein sorting.
Protein sorting can be of two types: signal-based sorting and vesicle-based trafficking. In signal-based sorting, specific amino acid sequences called sorting signals target proteins to the proper location inside the cell either via gated transport or by protein translocation.  In gated transport, folded...

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Related Experiment Video

Updated: May 16, 2026

Single-Molecule Diffusion and Assembly on Polymer-Crowded Lipid Membranes
10:43

Single-Molecule Diffusion and Assembly on Polymer-Crowded Lipid Membranes

Published on: July 19, 2022

Disordered Protein Diffusion under Crowded Conditions.

Yaqiang Wang1, Laura A Benton, Vishavpreet Singh

  • 1Chemistry, University of North Carolina, Chapel Hill, NC 27599.

The Journal of Physical Chemistry Letters
|November 28, 2012
PubMed
Summary
This summary is machine-generated.

Protein shape significantly influences diffusion, especially in crowded cellular environments. Intrinsically disordered proteins diffuse faster than globular ones under crowding, contrary to dilute solutions.

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4D Imaging of Protein Aggregation in Live Cells
08:59

4D Imaging of Protein Aggregation in Live Cells

Published on: April 5, 2013

Related Experiment Videos

Last Updated: May 16, 2026

Single-Molecule Diffusion and Assembly on Polymer-Crowded Lipid Membranes
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Published on: July 19, 2022

Single-Molecule Tracking Microscopy - A Tool for Determining the Diffusive States of Cytosolic Molecules
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4D Imaging of Protein Aggregation in Live Cells
08:59

4D Imaging of Protein Aggregation in Live Cells

Published on: April 5, 2013

Area of Science:

  • Biophysics
  • Molecular Biology
  • Protein Dynamics

Background:

  • Intrinsically disordered proteins (IDPs) play crucial roles in cellular signaling, regulation, and translocation.
  • Understanding the diffusion of IDPs under physiological conditions is key to elucidating their functions.
  • Macromolecular crowding significantly impacts protein behavior and dynamics within cells.

Purpose of the Study:

  • To quantify and compare the translational diffusion of a globular protein and an intrinsically disordered protein.
  • To investigate the effects of macromolecular crowding on protein diffusion.
  • To determine the role of protein shape in diffusion dynamics under crowded conditions.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) spectroscopy was employed to measure translational diffusion.
  • Experiments were conducted on chymotrypsin inhibitor 2 (CI2, a globular protein) and alpha-synuclein (a disordered protein).
  • Diffusion was assessed in both dilute solutions and under conditions mimicking cellular crowding.

Main Results:

  • In dilute solution, the smaller globular protein CI2 diffused faster than the larger disordered protein alpha-synuclein.
  • Under crowded conditions, alpha-synuclein exhibited faster diffusion than CI2, despite its larger size.
  • These findings highlight a reversal of diffusion behavior dependent on the cellular environment.

Conclusions:

  • Protein shape is a critical determinant of diffusion rates in crowded biological environments.
  • Macromolecular crowding alters diffusion dynamics, favoring faster movement for disordered proteins.
  • The results provide insights into the functional advantages of disordered protein structures in cellular signaling.