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Related Concept Videos

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...
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...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Aromatic Hydrocarbon Cations: Structural Overview01:18

Aromatic Hydrocarbon Cations: Structural Overview

Cycloheptatriene is a neutral monocyclic unsaturated hydrocarbon that consists of an odd number of carbon atoms and an intervening sp3 carbon in the ring. The three double bonds in the ring correspond to 6 π electrons, which is a Huckel number, and therefore satisfies the criteria of 4n + 2 π electrons. However, the intervening sp3 carbon disrupts the continuous overlap of p orbitals. As a result, cycloheptatriene is not aromatic.
Removing one hydrogen from the intervening CH2 group with both...

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Related Experiment Video

Updated: May 23, 2026

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
06:45

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay

Published on: May 26, 2011

Aromatically functionalized cyclic tricholate macrocycles: aggregation, transmembrane pore formation, flexibility,

Lakmini Widanapathirana1, Yan Zhao

  • 1Department of Chemistry, Iowa State University, Ames, Iowa 50011-3111, United States.

The Journal of Organic Chemistry
|April 25, 2012
PubMed
Summary
This summary is machine-generated.

Macrocyclic oligocholates form transmembrane nanopores in lipid membranes. This self-assembly is driven by solvophobic effects and molecular stacking, influenced by macrocycle structure and aromatic interactions.

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Self-assembling Morphologies Obtained from Helical Polycarbodiimide Copolymers and Their Triazole Derivatives

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Last Updated: May 23, 2026

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
06:45

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay

Published on: May 26, 2011

Controlling the Size, Shape and Stability of Supramolecular Polymers in Water
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Controlling the Size, Shape and Stability of Supramolecular Polymers in Water

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Self-assembling Morphologies Obtained from Helical Polycarbodiimide Copolymers and Their Triazole Derivatives
09:22

Self-assembling Morphologies Obtained from Helical Polycarbodiimide Copolymers and Their Triazole Derivatives

Published on: February 7, 2017

Area of Science:

  • Supramolecular Chemistry
  • Materials Science
  • Biophysics

Background:

  • Macrocyclic compounds are investigated for their self-assembly properties.
  • Understanding molecular aggregation in lipid membranes is crucial for drug delivery and biomimetic systems.

Purpose of the Study:

  • To investigate the aggregation behavior of macrocyclic oligocholates in solution and lipid membranes.
  • To elucidate the driving forces and structural factors governing transmembrane nanopore formation.

Main Methods:

  • Fluorescence spectroscopy was employed to study molecular interactions.
  • Liposome leakage assays were used to assess membrane disruption and pore formation.

Main Results:

  • Solvophobically driven aggregation of macrocycles occurred in lipid membranes.
  • Macrocycles stacked to form transmembrane nanopores, facilitated by water molecule aggregation in nonpolar environments.
  • Smaller, rigid macrocycles exhibited superior stacking compared to larger, flexible ones.
  • Naphthalenediimide (NDI) acceptor-acceptor interactions were more effective for pore formation than pyrene-NDI donor-acceptor interactions.

Conclusions:

  • Macrocyclic oligocholate aggregation in membranes is driven by hydrophobic effects and molecular stacking.
  • Macrocycle rigidity and the nature of aromatic interactions significantly impact transmembrane pore formation.
  • These findings offer insights into designing self-assembling systems for potential applications.