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Characterization of G-Quadruplexes Folding/Unfolding Dynamics and Interactions with Proteins from Single-Molecule Force Spectroscopy

期刊

BIOMOLECULES
卷 11, 期 11, 页码 -

出版社

MDPI
DOI: 10.3390/biom11111579

关键词

single-molecule manipulations; G-quadruplex; polymorphism; kinetics; mechanical stability; G4 helicase; nucleic acid chaperone

资金

  1. National Natural Science Foundation of China [32171225]

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G-quadruplexes (G4s) are stable secondary nucleic acid structures that are crucial in biological processes, with complex folding/unfolding dynamics. Single-molecule force spectroscopy methods can be used to study their polymorphism and dynamics. Recent studies have utilized this approach to investigate the molecular mechanisms of G4-interacting proteins.
G-quadruplexes (G4s) are stable secondary nucleic acid structures that play crucial roles in many fundamental biological processes. The folding/unfolding dynamics of G4 structures are associated with the replication and transcription regulation functions of G4s. However, many DNA G4 sequences can adopt a variety of topologies and have complex folding/unfolding dynamics. Determining the dynamics of G4s and their regulation by proteins remains challenging due to the coexistence of multiple structures in a heterogeneous sample. Here, in this mini-review, we introduce the application of single-molecule force-spectroscopy methods, such as magnetic tweezers, optical tweezers, and atomic force microscopy, to characterize the polymorphism and folding/unfolding dynamics of G4s. We also briefly introduce recent studies using single-molecule force spectroscopy to study the molecular mechanisms of G4-interacting proteins.

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