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Related Concept Videos

Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
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Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
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Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
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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.
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Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
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Protein Complexes with Interchangeable Parts01:57

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Related Experiment Video

Updated: May 16, 2026

Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly
09:34

Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly

Published on: February 6, 2020

Sequence-dependent assembly to control molecular interface properties.

Graham de Ruiter1, Michal Lahav, Hodaya Keisar

  • 1Department of Organic Chemistry, Weizmann Institute of Science, Rehovot, Israel.

Angewandte Chemie (International Ed. in English)
|November 21, 2012
PubMed
Summary
This summary is machine-generated.

Altering the assembly sequence of metal complexes creates molecular materials with tunable electrochemical properties. This sequence-dependent self-assembly strategy offers control over electron transfer, current flow, and charge trapping for advanced materials design.

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Area of Science:

  • Materials Science
  • Electrochemistry
  • Supramolecular Chemistry

Background:

  • Self-assembly is crucial for creating advanced molecular materials.
  • Controlling the properties of these materials often relies on precise structural organization.
  • Isostructural metal complexes offer a platform for studying sequence-dependent assembly.

Purpose of the Study:

  • To investigate how the assembly sequence of isostructural metal complexes influences resulting molecular material properties.
  • To demonstrate the tunability of electrochemical characteristics through sequence control.
  • To highlight the broad applicability of sequence-dependent assembly strategies.

Main Methods:

  • Layer-by-layer assembly of two isostructural metal complexes.
  • Electrochemical characterization of the resulting molecular materials.
  • Analysis of structure-property relationships based on assembly order.

Main Results:

  • Assembly sequence dictates the electrochemical behavior of the molecular materials.
  • Observed properties include reversible electron transfer, unidirectional current flow, and charge trapping.
  • Materials exhibit distinct electronic functionalities based on the specific layer arrangement.

Conclusions:

  • The sequence of assembly is a critical design parameter for molecular materials.
  • Sequence-dependent self-assembly provides a versatile route to engineer specific electrochemical functions.
  • This approach has significant implications for fields utilizing self-assembly, such as electronics and sensing.