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Related Concept Videos

Protein Diffusion in the Membrane01:24

Protein Diffusion in the Membrane

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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...
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Diffusion01:12

Diffusion

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Diffusion is the passive movement of substances down their concentration gradients—requiring no expenditure of cellular energy. Substances, such as molecules or ions, diffuse from an area of high concentration to an area of low concentration in the cytosol or across membranes. Eventually, the concentration will even out, with the substance moving randomly but causing no net change in concentration. Such a state is called dynamic equilibrium, which is essential for maintaining overall...
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Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
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Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
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A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
Targeting proteins to the ER
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Nuclear encoded mitochondrial precursors are imported to the inner membrane in a multistep process involving two separate translocons, TIM22 and TIM23. TIM23 is a cation-selective pore that remains closed by the N terminal segment of the protein. Negative charges on the TIM23 act as a receptor for the incoming precursor, pulling the positively charged matrix-targeting sequence for peptide insertion and translocation.
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Author Spotlight: Evaluation of Protein-Condensate Dynamics in Live Human Cells
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Peptide diffusion in biomolecular condensates.

Riley J Workman1, Caleb J Huang1, Gillian C Lynch1

  • 1University of Texas Medical Branch, 301 University Boulevard, Galveston, Texas.

Biophysical Journal
|May 16, 2024
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Summary
This summary is machine-generated.

Biomolecular diffusion in liquid-liquid phase-separated condensates is key for turnover. Peptide sequence and structure influence diffusion rates within these condensates, with compact structures showing the fastest movement.

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Area of Science:

  • Biophysics
  • Chemical Physics
  • Molecular Biology

Background:

  • Liquid-liquid phase separation (LLPS) is crucial for cellular organization.
  • Biomolecular diffusion within condensates governs their dynamic turnover.
  • Understanding diffusion dynamics is essential for cellular signaling and function.

Purpose of the Study:

  • To investigate the diffusion dynamics of model peptides within phase-separated condensates.
  • To determine how peptide sequence and conformational distribution affect diffusion coefficients.
  • To explore the implications for condensate turnover and cellular signaling.

Main Methods:

  • Atomic-level molecular dynamics simulations were employed.
  • Mean square displacement and diffusion constants were calculated.
  • Peptides (GGGGGG, GGQGG, GGVGG) in aqueous solutions undergoing phase separation were modeled.

Main Results:

  • Peptide solutions phase separated into aqueous and peptide-rich droplet phases.
  • Diffusion coefficients varied based on peptide state (solvated, surface, droplet).
  • Peptide sequence and conformational distribution significantly influenced diffusion, with sequence being dominant.

Conclusions:

  • Compact peptide structures exhibited the fastest diffusion in the peptide-rich condensate phase.
  • Peptide sequence is a primary determinant of diffusion rates and condensate turnover.
  • Findings offer insights into the dynamics of biomolecular condensates and signaling systems.