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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...

Protein Complexes with Interchangeable Parts

Protein Complexes with Interchangeable Parts

Protein Complex Assembly

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.
Many viruses self-assemble into a fully functional unit using the infected host cell to...

Protein Complex Assembly

Protein Complex Assembly

Conserved Binding Sites

Conserved Binding Sites

Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...

Conserved Binding Sites

Conserved Binding Sites

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Related Experiment Video

Updated: Apr 6, 2026

Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules

Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules

Published on: July 25, 2013

Fuzzy complexes: Specific binding without complete folding.

Rashmi Sharma¹, Zsolt Raduly¹, Marton Miskei¹

¹MTA-DE Momentum, Laboratory of Protein Dynamics, Department of Biochemistry and Molecular Biology, University of Debrecen, Hungary.

|July 31, 2015

Summary

This summary is machine-generated.

Protein complexes can be "fuzzy," retaining structural flexibility and forming transient contacts. This molecular fuzziness, often regulated by modifications, plays key roles in biological regulation and protein stability.

Keywords:

Conformational selection Fuzzy complex Intrinsically disordered protein Protein interaction Signal transduction Specificity Transcription regulation Viral protein

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Using In Vitro Fluorescence Resonance Energy Transfer to Study the Dynamics Of Protein Complexes at a Millisecond Time Scale

Using In Vitro Fluorescence Resonance Energy Transfer to Study the Dynamics Of Protein Complexes at a Millisecond Time Scale

Published on: March 14, 2019

Area of Science:

Biochemistry
Structural Biology
Molecular Biology

Background:

Molecular recognition traditionally assumes rigid structures and unambiguous interactions.
Emerging evidence reveals that protein complexes can exhibit structural multiplicity and dynamic disorder, a phenomenon termed 'fuzziness'.

Purpose of the Study:

To explore the concept of molecular fuzziness in protein complexes.
To discuss the implications of fuzziness in biological regulation and protein dynamics.

Main Methods:

Review of experimental evidence characterizing fuzzy protein complexes.
Analysis of the role of post-translational modifications and alternative splicing in tuning fuzzy interactions.

Main Results:

Fuzzy regions within protein complexes establish alternative, transient contacts.
Fuzziness is prevalent in complexes regulating gene expression, signal transduction, and cell cycle.
Fuzzy complexes are also found in viral proteins, cytoskeleton, and metabolic enzymes.

Conclusions:

Molecular fuzziness represents a significant departure from traditional models of specific molecular recognition.
This dynamic characteristic is actively modulated by nature to fine-tune binding affinities and biological functions.
Fuzziness may contribute to the stability of intrinsically disordered proteins.