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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...

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...

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.

Noncovalent Attractions in Biomolecules

Noncovalent Attractions in Biomolecules

Noncovalent attractions are associations within and between molecules that influence the shape and structural stability of complexes. These interactions differ from covalent bonding in that they do not involve sharing of electrons.
Four types of noncovalent interactions are hydrogen bonds, van der Waals forces, ionic bonds, and hydrophobic interactions.
Hydrogen bonding results from the electrostatic attraction of a hydrogen atom covalently bonded to a strong-electronegative atom like oxygen,...

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Related Experiment Video

Updated: May 24, 2026

Protein Complex Affinity Capture from Cryomilled Mammalian Cells

Protein Complex Affinity Capture from Cryomilled Mammalian Cells

Published on: December 9, 2016

"Fuzziness" in the celular interactome: a historical perspective.

G Rickey Welch¹

¹Department of Biological Sciences, University of Maryland, Baltimore, Maryland, USA. welch@umbc.edu

Advances in Experimental Medicine and Biology

|March 9, 2012

Summary

This summary is machine-generated.

The cellular protein-protein interactome, a key concept in systems biology, exhibits "fuzziness." Historical analysis clarifies interactome studies and the in vivo importance of protein interactions.

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Last Updated: May 24, 2026

Protein Complex Affinity Capture from Cryomilled Mammalian Cells

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Published on: December 9, 2016

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Area of Science:

Systems Biology
Molecular Biology
Bioinformatics

Background:

The cellular protein-protein interactome is a recent development in postgenomic systems biology.
Understanding protein interactions requires historical context.

Observation:

The concept of
fuzziness
in protein behavior, proposed by Tompa and Fuxreiter, provides a framework for analysis.
Controversies in interactome studies can be rationalized using this concept.

Findings:

Historical literature on protein-protein interactions, dating to the mid-1900s, is crucial.
This historical perspective clarifies the
fuzziness
observed in interactome data.
It establishes a basis for understanding the physiological importance of protein-protein interactions in vivo.

Implications:

Provides a historical framework for understanding the cellular protein-protein interactome.
Offers a new perspective on interpreting interactome study controversies.
Highlights the physiological significance of protein-protein interactions within a systems biology context.