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Related Concept Videos

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...
Fluid Mosaic Model01:19

Fluid Mosaic Model

Scientists identified the plasma membrane in the 1890s and its principal chemical components (lipids and proteins) by 1915. The model for plasma membrane structure, proposed in 1935 by Hugh Davson and James Danielli, was the first model to be widely accepted in the scientific community. The model was based on the plasma membrane's "railroad track" appearance in early electron micrographs. Davson and Danielli theorized that the plasma membrane's structure resembled a sandwich with the analogy of...
Fluid Mosaic Model01:34

Fluid Mosaic Model

The fluid mosaic model was first proposed as a visual representation of research observations. The model comprises the composition and dynamics of membranes and serves as a foundation for future membrane-related studies. The model depicts the structure of the plasma membrane with a variety of components, which include phospholipids, proteins, and carbohydrates. These integral molecules are loosely bound, defining the cell’s border and providing fluidity for optimal function.LipidsThe most...
Mechanisms of Membrane Domain Formation00:59

Mechanisms of Membrane Domain Formation

Different physical properties of lipids and proteins allow them to localize and form distinct islands or domains in the membrane. Some membrane domains are formed due to protein-protein interactions, whereas others are formed due to the presence of specific lipids such as sphingolipids and sterols—for example, large proteins, such as bacteriorhodopsin, aggregate and create distinct domains.
Another mechanism for membrane domain formation involves membrane proteins interacting with cytoskeletal...
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...
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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...

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4D Imaging of Protein Aggregation in Live Cells
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Published on: April 5, 2013

Disordered proteins: biological membranes as two-dimensional aggregation matrices.

Roberth Byström1, Christopher Aisenbrey, Tomasz Borowik

  • 1Department of Chemistry, Umeå University, 90187, Umeå, Sweden.

Cell Biochemistry and Biophysics
|November 1, 2008
PubMed
Summary

Biological membranes significantly influence protein misfolding in amyloid diseases. They promote aggregation and toxicity, acting as reactive interfaces that alter protein stability and aggregation rates.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Neuroscience

Background:

  • Aberrantly folded proteins are characteristic of amyloidogenic diseases.
  • The in vivo molecular mechanisms driving protein misfolding and cytotoxicity remain largely elusive.
  • The cellular environment critically influences protein fate and aggregation.

Purpose of the Study:

  • To review the role of biological membranes in protein misfolding and amyloidogenesis.
  • To explore how membranes affect protein conformational stability, aggregation kinetics, and toxicity.
  • To present a molecular concept of membrane-mediated protein misfolding.

Main Methods:

  • Review of recent research on amyloidogenic proteins, including amyloid-beta (Abeta) and medin.
  • Discussion of findings from novel NMR-based approaches for studying membrane-protein interactions.
  • Analysis of the influence of specific lipids, such as gangliosides, on protein aggregation.

Main Results:

  • Membranes directly promote the aggregation of amyloidogenic proteins like Abeta.
  • Specific lipids, such as neuronal gangliosides, enhance membrane-induced aggregation.
  • Membranes also influence the misfolding of soluble, non-amphipathic proteins.
  • Membrane-protein interactions are proposed to occur as a quasi-two-dimensional process.

Conclusions:

  • Biological membranes are crucial interfaces affecting protein folding, misfolding, and aggregation in vivo.
  • Understanding membrane-protein interactions is vital for deciphering amyloidogenic disease mechanisms.
  • This knowledge may lead to strategies for preventing toxic protein actions.