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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...
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...
Membrane Domains01:18

Membrane Domains

The membrane domains concentrate specific lipids and proteins at one place within the membrane, which helps in cell signaling, adhesion, and other critical cellular processes. These domains can differ in size, composition, function, and lifespan.
Protein Domains
The membrane comprises a group of distinct proteins responsible for carrying out a cell's specific function. For example, the plasma membrane of the human sperm, or a single germ cell, contains a unique set of proteins in the anterior...
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...
Theories of Dissolution: The Danckwerts' Model and Interfacial Barrier Model01:09

Theories of Dissolution: The Danckwerts' Model and Interfacial Barrier Model

Various dissolution theories provide insight into the factors that influence the dissolution rate. Danckwerts' Model suggests that turbulence, rather than a stagnant layer, characterizes the dissolution medium at the solid-liquid interface. In this model, the agitated solvent contains macroscopic packets that move to the interface via eddy currents, facilitating the absorption and delivery of the drug to the bulk solution. The regular replenishment of solvent packets maintains the concentration...
Assembly of Signaling Complexes01:30

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.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...

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Updated: May 15, 2026

Multiscale Structures Aggregated by Imprinted Nanofibers for Functional Surfaces
06:14

Multiscale Structures Aggregated by Imprinted Nanofibers for Functional Surfaces

Published on: September 11, 2018

Structural and functional analysis of multi-interface domains.

Liang Zhao1, Steven C H Hoi, Limsoon Wong

  • 1School of Computer Engineering, Nanyang Technological University, Singapore, Singapore.

Plos One
|December 29, 2012
PubMed
Summary
This summary is machine-generated.

Multi-interface protein domains act as hubs in interaction networks. This study identifies unique fingerprints for these interfaces, revealing their functional specificity and structural patterns useful for protein engineering.

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Using Informational Connectivity to Measure the Synchronous Emergence of fMRI Multi-voxel Information Across Time
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Multiscale Structures Aggregated by Imprinted Nanofibers for Functional Surfaces
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Using Informational Connectivity to Measure the Synchronous Emergence of fMRI Multi-voxel Information Across Time
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Published on: July 1, 2014

Area of Science:

  • Biochemistry
  • Structural Biology
  • Bioinformatics

Background:

  • Multi-interface domains are crucial hubs in protein-protein interaction networks.
  • These domains possess multiple binding sites with potentially distinct functions.

Purpose of the Study:

  • To develop a method for identifying fingerprints of multi-interface domains.
  • To associate these fingerprints with specific protein functions.
  • To analyze the structural patterns within multi-interface domains.

Main Methods:

  • Application of graph theory and algorithms.
  • Analysis of a large dataset of multi-interface proteins from the Protein Data Bank (PDB).

Main Results:

  • Approximately 40% of proteins exhibit multi-interface properties, but these domains constitute only 1.8% of all domains.
  • Distinctive fingerprints were identified for the interfaces of multi-interface domains, suggesting functional specificity.
  • Cooperative and distinctive structural patterns were observed within these multiple interfaces.

Conclusions:

  • Multi-interface domains display functionally specific interfaces characterized by unique fingerprints.
  • Identified structural patterns offer potential for protein engineering applications.
  • The study highlights the importance of multi-interface domains in biological networks.