Work

Navigating the complexities of multi-domain protein folding

Year: 2024

Type: review

Abstract: Proteome complexity has expanded tremendously over evolutionary time, enabling biological diversification. Much of this complexity is achieved by combining a limited set of structural units into long polypeptides. This widely used evolutionary strategy poses challenges for folding of the resulting multi-domain proteins. As a consequence, their folding differs from that of small single-domain proteins, which generally fold quickly and reversibly. Co-translational processes and chaperone interactions are important aspects of multi-domain protein folding. In this review, we discuss some of the recent experimental progress toward understanding these processes.

Source: Current Opinion in Structural Biology

DOI: 10.1016/j.sbi.2024.102790

Authors: Nandakumar Rajasekaran, Christian M. Kaiser

Institutions: Johns Hopkins University, Utrecht University

Language: English

Topic: Protein Structure and Dynamics

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: hybrid

Estimated APC paid: $4,530

Funders: National Institutes of Health, National Institute of General Medical Sciences