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Protein-protein Interfaces

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...

Covalently Linked Protein Regulators

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.

Covalently Linked Protein Regulators

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.

Protein Networks

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 Complexes with Interchangeable Parts

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.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...

Protein Complexes with Interchangeable Parts

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.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...

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Updated: Jun 24, 2026

The Multifaceted Benefits of Protein Co-expression in Escherichia coli

The Multifaceted Benefits of Protein Co-expression in Escherichia coli

Published on: February 5, 2015

Deciphering peculiar protein-protein interacting modules in Deinococcus radiodurans.

Karim Mezhoud¹, Haïtham Sghaier, Insaf Barkallah

¹Unit of Microbiology and Molecular Biology, National Center for Nuclear Sciences and Technologies (CNSTN), Sidi Thabet Technopark, 2020, Ariana, Tunisia. kmezhoud@gmail.com

|April 10, 2009

Summary

Ionizing-radiation-resistant bacteria (IRRB) possess unique protein interactions that aid survival. This study identified novel protein interactions in DNA repair and metabolism pathways crucial for radiation resistance in Deinococcus radiodurans R1.

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Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

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Identification of Protein Complexes in Escherichia coli using Sequential Peptide Affinity Purification in Combination with Tandem Mass Spectrometry

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Published on: November 12, 2012

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues

Published on: July 14, 2015

Area of Science:

Microbiology
Molecular Biology
Biochemistry

Background:

Ionizing-radiation-resistant bacteria (IRRB), like Deinococcus radiodurans R1 (Deira), exhibit remarkable resistance to radiation.
Understanding the molecular mechanisms, particularly protein interactions, is key to explaining this resistance.

Purpose of the Study:

To predict and identify novel protein-protein interactions in IRRB.
To investigate the role of these interactions in cellular pathways associated with radiation resistance.

Main Methods:

Utilized the Database of Interacting Proteins (DIP) and the Protein Structural Interactome (PSI)-base server.
Predicted interactions of orthologs from 58 positively selected proteins in Deira and other IRRB, absent in ionizing-radiation-sensitive bacteria (IRSB).

Main Results:

Identified 18 novel domains and their interactomes involved in key biological processes.
These processes include DNA checkpoint and repair, kinase pathways, and energy/nucleotide metabolism.

Conclusions:

The identified protein interactomes offer new insights into the cellular pathways conferring ionizing-radiation resistance.
These findings highlight specific pathways critical for Deira's survival under high radiation conditions.