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Related Concept Videos

Protein Folding01:25

Protein Folding

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.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Folding01:22

Protein Folding

Overview
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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...
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...
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...
Multi-pass Transmembrane Proteins and β-barrels01:09

Multi-pass Transmembrane Proteins and β-barrels

In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as G-protein-linked receptors (GPCRs) and...

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Related Experiment Video

Updated: May 10, 2026

Native Cell Membrane Nanoparticles System for Membrane Protein-Protein Interaction Analysis
07:31

Native Cell Membrane Nanoparticles System for Membrane Protein-Protein Interaction Analysis

Published on: July 16, 2020

Engineered nanostructured β-sheet peptides protect membrane proteins.

Houchao Tao1, Sung Chang Lee, Arne Moeller

  • 1Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, California, USA.

Nature Methods
|July 3, 2013
PubMed
Summary
This summary is machine-generated.

New beta-strand peptides stabilize integral membrane proteins (IMPs). These peptides prevent aggregation, allowing for clear visualization of dynamic protein structures like the ABC transporter MsbA.

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A Tripeptide-Stabilized Nanoemulsion of Oleic Acid
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A Tripeptide-Stabilized Nanoemulsion of Oleic Acid

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Last Updated: May 10, 2026

Native Cell Membrane Nanoparticles System for Membrane Protein-Protein Interaction Analysis
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Published on: July 16, 2020

A Tripeptide-Stabilized Nanoemulsion of Oleic Acid
10:42

A Tripeptide-Stabilized Nanoemulsion of Oleic Acid

Published on: February 27, 2019

Area of Science:

  • Biochemistry
  • Structural Biology
  • Protein Science

Background:

  • Integral membrane proteins (IMPs) are crucial for cellular functions but challenging to study due to their hydrophobic nature and tendency to aggregate.
  • Stabilizing IMPs is essential for structural and functional characterization, particularly for dynamic proteins.

Purpose of the Study:

  • To design and characterize novel beta-strand peptides capable of stabilizing IMPs.
  • To assess the ability of these peptides to prevent IMP aggregation and facilitate visualization.

Main Methods:

  • Design of self-assembling beta-strand peptides.
  • Characterization of peptide-IMP complexes in solution and detergent-free buffer.
  • Electron microscopy for visualizing stabilized IMPs.

Main Results:

  • Beta-strand peptides self-assemble into filaments in solution.
  • Peptide association restructures IMPs, forming stable complexes resistant to aggregation.
  • Stable, single IMP-beta-strand peptide particles were visualized with low detergent background via electron microscopy.
  • Flexible conformations of the ATP-binding cassette (ABC) transporter MsbA were clearly visualized.

Conclusions:

  • Beta-strand peptides are effective tools for stabilizing integral membrane proteins.
  • This approach overcomes common challenges in IMP structural studies, enabling visualization of dynamic states.
  • The method provides a new avenue for studying the structure and function of challenging membrane proteins.