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Protein Complexes with Interchangeable Parts

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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

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Proteins are polymers of amino acids linked together by peptide bonds. Proteins and polypeptides are interchangeably used to refer to long chains of amino acids. However, polypeptides have a molecular weight of fewer than 10,000 daltons, while proteins have greater molecular weight. Polypeptides with less than 20 amino acids are called oligopeptides or simply peptides. Interactions among the constituent amino acid side chains of proteins help them fold into a stable 3-dimensional...

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Proteins: molecules defined by their trade-offs.

Lavi S Bigman¹, Yaakov Levy¹

¹Department of Structural Biology, Weizmann Institute of Science, Rehovot 76100, Israel.

Current Opinion in Structural Biology

|December 10, 2019

Summary

Protein structure and function involve trade-offs between conflicting forces, impacting stability, flexibility, and folding. Quantifying these biophysical trade-offs is essential for a complete understanding of protein behavior.

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Area of Science:

Biophysics
Structural Biology
Protein Science

Background:

Proteins are complex molecules governed by competing forces during folding and function.
These forces create trade-offs, such as stability versus flexibility, and function versus folding kinetics.
Understanding these trade-offs is crucial for deciphering protein behavior.

Purpose of the Study:

To highlight the inherent trade-offs in protein biophysics.
To emphasize the necessity of quantifying these conflicting forces.
To underscore the importance of these trade-offs for protein structure and function.

Main Methods:

This study is a conceptual analysis and review.
It synthesizes existing knowledge on protein biophysics and trade-offs.
No new experimental data were generated.

Main Results:

Proteins balance enthalpy and entropy during folding, with implications for stability.
Increased protein stability can lead to decreased flexibility, potentially hindering allosteric regulation.
Stability-function trade-offs can limit the acquisition of novel protein functions and affect folding mechanisms.

Conclusions:

Understanding protein biophysics requires quantifying the driving forces behind various trade-offs.
Quantification of these interconnected trade-offs is key to a comprehensive understanding of protein structure, function, and evolution.
Addressing these trade-offs is vital for protein engineering and drug design.