Backbone interactions and secondary structures in phase separation of disordered proteins

Biochem Soc Trans. 2024 Feb 13:BST20230618. doi: 10.1042/BST20230618. Online ahead of print.ABSTRACTIntrinsically disordered proteins (IDPs) are one of the major drivers behind the formation and characteristics of biomolecular condensates. Due to their inherent flexibility, the backbones of IDPs are significantly exposed, rendering them highly influential and susceptible to biomolecular phase separation. In densely packed condensates, exposed backbones have a heightened capacity to interact with neighboring protein chains, which might lead to strong coupling between the secondary structures and phase separation and further modulate the subsequent transitions of the condensates, such as aging and fibrillization. In this mini-review, we provide an overview of backbone-mediated interactions and secondary structures within biomolecular condensates to underscore the importance of protein backbones in phase separation. We further focus on recent advances in experimental techniques and molecular dynamics simulation methods for probing and exploring the roles of backbone interactions and secondary structures in biomolecular phase separation involving IDPs.PMID:38348795 | DOI:10.1042/BST20230618

Source: Biochemical Society Transactions - February 13, 2024 Category: Biochemistry Authors: Shanlong Li Yumeng Zhang Jianhan Chen Source Type: research