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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...
Protein Networks02:26

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
Protein Networks02:26

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
Cotranslational Protein Translocation01:20

Cotranslational Protein Translocation

Translocation of proteins across membranes is an ancient process that occurs even in bacteria and archaebacteria. In fact, the components of the translocation machinery are still conserved between prokaryotes and eukaryotes.
Sec61 channel partners for cotranslational translocation
During cotranslational translocation, the Sec61 channel partners with the signal recognition particle (SRP), the signal recognition particle receptor (SR), and the ribosomes to transport the nascent polypeptide chain...
Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the translocon complex.

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Related Experiment Video

Updated: May 31, 2026

Imaging Protein-protein Interactions in vivo
11:15

Imaging Protein-protein Interactions in vivo

Published on: October 10, 2010

Transient protein-protein interactions.

Saliha Ece Acuner Ozbabacan1, Hatice Billur Engin, Attila Gursoy

  • 1Center for Computational Biology and Bioinformatics, College of Engineering, Koc University, Istanbul, Turkey.

Protein Engineering, Design & Selection : PEDS
|June 17, 2011
PubMed
Summary

Transient protein-protein interactions (TPPIs) are vital in cells and can be drug targets. Understanding their structure and kinetics aids in designing new therapies.

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Last Updated: May 31, 2026

Imaging Protein-protein Interactions in vivo
11:15

Imaging Protein-protein Interactions in vivo

Published on: October 10, 2010

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

Quantification of Protein Interaction Network Dynamics using Multiplexed Co-Immunoprecipitation
07:57

Quantification of Protein Interaction Network Dynamics using Multiplexed Co-Immunoprecipitation

Published on: August 21, 2019

Area of Science:

  • Biochemistry and Molecular Biology
  • Structural Biology
  • Pharmacology

Background:

  • Transient complexes play critical roles in cellular biochemical pathways and signaling cascades.
  • These transient interactions are increasingly recognized as important targets for therapeutic drug development.
  • A detailed molecular understanding of transient protein-protein interactions (TPPIs) is essential for biological insight and drug design.

Purpose of the Study:

  • To provide a comprehensive overview of transient interactions, their significance as drug targets, and their structural characterization.
  • To highlight the necessity of a molecular perspective on protein-protein interfaces for understanding and designing TPPIs.
  • To review experimental and computational methods for detecting, classifying, and predicting TPPIs.

Main Methods:

  • Structural characterization based on geometrical and physicochemical features of transient complex interfaces.
  • Introduction to the association kinetics governing TPPIs.
  • Elaboration on experimental techniques for detecting TPPIs and computational methods for classification.

Main Results:

  • Compilation of currently available databases and servers for identifying and predicting TPPIs.
  • Discussion on the importance of high-quality structures for understanding protein-protein interactions.
  • Overview of methods to analyze transient complex interfaces.

Conclusions:

  • Understanding the structural and kinetic properties of TPPIs is crucial for biological processes and drug discovery.
  • A combination of experimental and computational approaches is necessary for characterizing and predicting transient interactions.
  • Available resources can aid researchers in identifying and predicting TPPIs for further study.