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Annual Review of Biophysics

Volume 53, 2024

Biophysical Principles Emerging from Experiments on Protein–Protein Association and Aggregation

Abstract

Protein–protein association and aggregation are fundamental processes that play critical roles in various biological phenomena, from cellular signaling to disease progression. Understanding the underlying biophysical principles governing these processes is crucial for elucidating their mechanisms and developing strategies for therapeutic intervention. In this review, we provide an overview of recent experimental studies focused on protein–protein association and aggregation. We explore the key biophysical factors that influence these processes, including protein structure, conformational dynamics, and intermolecular interactions. We discuss the effects of environmental conditions such as temperature, pH and related buffer-specific effects, and ionic strength and related ion-specific effects on protein aggregation. The effects of polymer crowders and sugars are also addressed. We list the techniques used to study aggregation. We analyze emerging trends and challenges in the field, including the development of computational models and the integration of multidisciplinary approaches for a comprehensive understanding of protein–protein association and aggregation.

Keyword(s): buffer-specific effects, ion-specific effects, liquid–liquid phase separation, protein aggregation, protein–protein interactions, theoretical modeling
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/content/journals/10.1146/annurev-biophys-030722-111729
2024-07-16
2024-10-06
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/content/journals/10.1146/annurev-biophys-030722-111729
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Biophysical Principles Emerging from Experiments on Protein–Protein Association and Aggregation
Annual Review of Biophysics 53, 1 (2024); https://doi.org/10.1146/annurev-biophys-030722-111729
/content/journals/10.1146/annurev-biophys-030722-111729
/content/journals/10.1146/annurev-biophys-030722-111729
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